S00033
type: Enzyme
rlcp: p10515
cath: Cytochrome p450
ec: https://purl.uniprot.org/enzyme/1.14.15.1
csa: 1akd
macie: M0133
uniprot: P00183
kegg enzyme: methylene monooxygenase
kegg cofactor: Heme
kegg substrate: (+)-Camphor
kegg substrate: Putidaredoxin
kegg substrate: O2
kegg product: (+)-exo-5-Hydroxycamphor
kegg product: Oxidized putidaredoxin
kegg product: H2O
pdb: 1akdA
pdb: 1c8jA
pdb: 1c8jB
pdb: 1cp4A
pdb: 1dz4A
pdb: 1dz4B
pdb: 1dz6A
pdb: 1dz6B
pdb: 1dz8A
pdb: 1dz8B
pdb: 1dz9A
pdb: 1dz9B
pdb: 1gebA
pdb: 1gekA
pdb: 1gemA
pdb: 1gjmA
pdb: 1iwiA
pdb: 1iwjA
pdb: 1iwkA
pdb: 1j51A
pdb: 1j51B
pdb: 1j51C
pdb: 1j51D
pdb: 1k2oA
pdb: 1k2oB
pdb: 1lwlA
pdb: 1mpwA
pdb: 1mpwB
pdb: 1nooA
pdb: 1o76A
pdb: 1o76B
pdb: 1p2yA
pdb: 1p7rA
pdb: 1phaA
pdb: 1phbA
pdb: 1phcA
pdb: 1phdA
pdb: 1pheA
pdb: 1phfA
pdb: 1phgA
pdb: 1qmqA
pdb: 1re9A
pdb: 1rf9A
pdb: 1t85A
pdb: 1t86A
pdb: 1t86B
pdb: 1t87A
pdb: 1t87B
pdb: 1t88A
pdb: 1t88B
pdb: 1uyuA
pdb: 1uyuB
pdb: 1yrcA
pdb: 1yrdA
pdb: 2a1mA
pdb: 2a1mB
pdb: 2a1nA
pdb: 2a1nB
pdb: 2a1oA
pdb: 2a1oB
pdb: 2cp4A
pdb: 2cppA
pdb: 2fe6A
pdb: 2ferA
pdb: 2feuA

Cytochrome p450
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.630.10
catalytic domain: index.html

Heme
type: KeggCofactor
references: KEGG:C00032
references: CHEBI:17627
references: CHEBI:26355
compound type: aromatic ring (with nitrogen atoms)
compound type: carboxyl group
compound type: heavy metal

(+)-Camphor
type: KeggSubstrate
references: KEGG:C00808
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate

Putidaredoxin
type: KeggSubstrate
references: KEGG:C02069
compound type: heavy metal
compound type: peptide/protein
compound type: sulfide group

O2
type: KeggSubstrate
references: KEGG:C00007
references: CHEBI:15379
references: CHEBI:26689
references: CHEBI:27140
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: others

(+)-exo-5-Hydroxycamphor
type: KeggProduct
references: KEGG:C03448
references: CHEBI:20570
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate

Oxidized putidaredoxin
type: KeggProduct
references: KEGG:C03302
compound type: heavy metal
compound type: peptide/protein
compound type: sulfide group

H2O
type: KeggProduct
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: H2O

1akdA
type: Pdb
references: 1akd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1akd
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1c8jA
type: Pdb
references: 1c8j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c8j
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F

1c8jB
type: Pdb
references: 1c8j
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c8j
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F

1cp4A
type: Pdb
references: 1cp4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cp4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz4A
type: Pdb
references: 1dz4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz4B
type: Pdb
references: 1dz4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz6A
type: Pdb
references: 1dz6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz6
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz6B
type: Pdb
references: 1dz6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz6
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz8A
type: Pdb
references: 1dz8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz8
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz8B
type: Pdb
references: 1dz8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz8
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz9A
type: Pdb
references: 1dz9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz9
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1dz9B
type: Pdb
references: 1dz9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dz9
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1gebA
type: Pdb
references: 1geb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geb
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;
cofactor binding residue: CYS 357(Iron binding)
comment: mutant T252I

1gekA
type: Pdb
references: 1gek
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gek
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1gemA
type: Pdb
references: 1gem
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gem
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1gjmA
type: Pdb
references: 1gjm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gjm
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1iwiA
type: Pdb
references: 1iwi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iwi
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1iwjA
type: Pdb
references: 1iwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iwj
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant R109K

1iwkA
type: Pdb
references: 1iwk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iwk
catalytic residue: ;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant R112K

1j51A
type: Pdb
references: 1j51
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j51
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87Y, Y96F, V247L, C334A

1j51B
type: Pdb
references: 1j51
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j51
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87Y, Y96F, V247L, C334A

1j51C
type: Pdb
references: 1j51
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j51
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87Y, Y96F, V247L, C334A

1j51D
type: Pdb
references: 1j51
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j51
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87Y, Y96F, V247L, C334A

1k2oA
type: Pdb
references: 1k2o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k2o
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutation C334A

1k2oB
type: Pdb
references: 1k2o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1k2o
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutation C334A

1lwlA
type: Pdb
references: 1lwl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lwl
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1mpwA
type: Pdb
references: 1mpw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mpw
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, V247L, C334A

1mpwB
type: Pdb
references: 1mpw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mpw
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, V247L, C334A

1nooA
type: Pdb
references: 1noo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1noo
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1o76A
type: Pdb
references: 1o76
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o76
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1o76B
type: Pdb
references: 1o76
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1o76
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1p2yA
type: Pdb
references: 1p2y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p2y
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1p7rA
type: Pdb
references: 1p7r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p7r
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1phaA
type: Pdb
references: 1pha
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pha
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1phbA
type: Pdb
references: 1phb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phb
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1phcA
type: Pdb
references: 1phc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phc
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1phdA
type: Pdb
references: 1phd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phd
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1pheA
type: Pdb
references: 1phe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phe
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1phfA
type: Pdb
references: 1phf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phf
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1phgA
type: Pdb
references: 1phg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phg
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1qmqA
type: Pdb
references: 1qmq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qmq
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A

1re9A
type: Pdb
references: 1re9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1re9
catalytic residue: ARG 102;LYS 168;ARG 176;ASP 241;THR 242
cofactor binding residue: CYS 347(Iron binding)

1rf9A
type: Pdb
references: 1rf9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rf9
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1t85A
type: Pdb
references: 1t85
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t85
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A, L358P

1t86A
type: Pdb
references: 1t86
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t86
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A, L358P

1t86B
type: Pdb
references: 1t86
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t86
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A, L358P

1t87A
type: Pdb
references: 1t87
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t87
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A

1t87B
type: Pdb
references: 1t87
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t87
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A

1t88A
type: Pdb
references: 1t88
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t88
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A

1t88B
type: Pdb
references: 1t88
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t88
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant C334A

1uyuA
type: Pdb
references: 1uyu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uyu
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1uyuB
type: Pdb
references: 1uyu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1uyu
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1yrcA
type: Pdb
references: 1yrc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yrc
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

1yrdA
type: Pdb
references: 1yrd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yrd
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2a1mA
type: Pdb
references: 2a1m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a1m
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2a1mB
type: Pdb
references: 2a1m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a1m
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2a1nA
type: Pdb
references: 2a1n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a1n
catalytic residue: ARG 112;LYS 178;ARG 186; ;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant D251N

2a1nB
type: Pdb
references: 2a1n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a1n
catalytic residue: ARG 112;LYS 178;ARG 186; ;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant D251N

2a1oA
type: Pdb
references: 2a1o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a1o
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;
cofactor binding residue: CYS 357(Iron binding)
comment: mutant T252A

2a1oB
type: Pdb
references: 2a1o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a1o
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;
cofactor binding residue: CYS 357(Iron binding)
comment: mutant T252A

2cp4A
type: Pdb
references: 2cp4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cp4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;
cofactor binding residue: CYS 357(Iron binding)
comment: mutant T252A

2cppA
type: Pdb
references: 2cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2fe6A
type: Pdb
references: 2fe6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fe6
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2ferA
type: Pdb
references: 2fer
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fer
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2feuA
type: Pdb
references: 2feu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2feu
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2feuB
type: Pdb
references: 2feu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2feu
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2frzA
type: Pdb
references: 2frz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2frz
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, V247L, C334A

2frzB
type: Pdb
references: 2frz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2frz
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, V247L, C334A

2gqxA
type: Pdb
references: 2gqx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gqx
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, L244A, V247L, C334A

2gqxB
type: Pdb
references: 2gqx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gqx
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, L244A, V247L, C334A

2gr6A
type: Pdb
references: 2gr6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gr6
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, L244A, V247L, C334A

2gr6B
type: Pdb
references: 2gr6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gr6
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant F87W, Y96F, L244A, V247L, C334A

2h7qA
type: Pdb
references: 2h7q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2h7q
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2h7rA
type: Pdb
references: 2h7r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2h7r
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant L244A

2h7sA
type: Pdb
references: 2h7s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2h7s
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant L244A

2h7sC
type: Pdb
references: 2h7s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2h7s
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant L244A

2qblA
type: Pdb
references: 2qbl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qbl
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant G248T

2qbmA
type: Pdb
references: 2qbm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qbm
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant G248T

2qbnA
type: Pdb
references: 2qbn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qbn
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant G248V

2qboA
type: Pdb
references: 2qbo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qbo
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant G248V

2zawA
type: Pdb
references: 2zaw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zaw
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

2zaxA
type: Pdb
references: 2zax
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zax
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

3cp4A
type: Pdb
references: 3cp4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3cp4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

3cppA
type: Pdb
references: 3cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

4cp4A
type: Pdb
references: 4cp4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4cp4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

4cppA
type: Pdb
references: 4cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

5cp4A
type: Pdb
references: 5cp4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5cp4
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

5cppA
type: Pdb
references: 5cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

6cp4A
type: Pdb
references: 6cp4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6cp4
catalytic residue: ARG 112;LYS 178;ARG 186; ;THR 252
cofactor binding residue: CYS 357(Iron binding)
comment: mutant D251N

6cppA
type: Pdb
references: 6cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

7cppA
type: Pdb
references: 7cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

8cppA
type: Pdb
references: 8cpp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8cpp
catalytic residue: ARG 112;LYS 178;ARG 186;ASP 251;THR 252
cofactor binding residue: CYS 357(Iron binding)

Analogue
compound: (+)-Camphor
pdb: 1j51A
ligand het code: TCZ

Analogue
compound: (+)-Camphor
pdb: 1j51B
ligand het code: TCZ

Analogue
compound: (+)-Camphor
pdb: 1j51C
ligand het code: TCZ

Analogue
compound: (+)-Camphor
pdb: 1k2oA
ligand het code: RFA-RFB

Analogue
compound: (+)-Camphor
pdb: 1k2oB
ligand het code: RFA-RFB

Analogue
compound: (+)-Camphor
pdb: 1lwlA
ligand het code: DSO

Analogue
compound: (+)-Camphor
pdb: 1p7rA
ligand het code: NCT

Analogue
compound: (+)-Camphor
pdb: 1pheA
ligand het code: PIM

Analogue
compound: (+)-Camphor
pdb: 1qmqA
ligand het code: LRB-DRB

Analogue
compound: (+)-Camphor
pdb: 1re9A
ligand het code: DSO

Analogue
compound: (+)-Camphor
pdb: 1rf9A
ligand het code: DBR

Analogue
compound: (+)-Camphor
pdb: 2gqxA
ligand het code: 5CL

Analogue
compound: (+)-Camphor
pdb: 3cp4A
ligand het code: ADM

Analogue
compound: (+)-Camphor
pdb: 4cppA
ligand het code: ADM

Analogue
compound: (+)-Camphor
pdb: 5cppA
ligand het code: ADO

Analogue
compound: (+)-Camphor
pdb: 6cppA
ligand het code: CAE

Analogue
compound: (+)-Camphor
pdb: 7cppA
ligand het code: NCM

Analogue
compound: O2
pdb: 1o76A
ligand het code: CYN

Analogue
compound: O2
pdb: 1o76B
ligand het code: CYN

Analogue
compound: O2
pdb: 1t85A
ligand het code: CMO

Analogue
compound: O2
pdb: 1t87B
ligand het code: CMO

Analogue
compound: O2
pdb: 2qbmA
ligand het code: CYN

Analogue
compound: O2
pdb: 2qboA
ligand het code: CYN

Analogue
compound: O2
pdb: 3cppA
ligand het code: CMO

Analogue
compound: Heme
pdb: 1cp4A
ligand het code: HEM-BNZ

Analogue
compound: Heme
pdb: 1gekA
ligand het code: HEM-NBN

Analogue
compound: Heme
pdb: 1gemA
ligand het code: HEM-NBN

Analogue
compound: Heme
pdb: 1p2yA
ligand het code: HEM-NCT

Analogue
compound: Heme
pdb: 1phaA
ligand het code: HEM-PFZ

Analogue
compound: Heme
pdb: 1phbA
ligand het code: HEM-PFZ

Analogue
compound: Heme
pdb: 1phdA
ligand het code: HEM-PIM

Analogue
compound: Heme
pdb: 1phfA
ligand het code: HEM-PIM

Analogue
compound: Heme
pdb: 1phgA
ligand het code: HEM-MYT

Analogue
compound: Heme
pdb: 2fe6A
ligand het code: MNR

Analogue
compound: Heme
pdb: 2ferA
ligand het code: MNR

Analogue
compound: Heme
pdb: 2feuA
ligand het code: MNR

Analogue
compound: Heme
pdb: 2feuB
ligand het code: MNR

Analogue
compound: Heme
pdb: 2h7qA
ligand het code: HEM-IMD

Analogue
compound: Heme
pdb: 2h7rA
ligand het code: HEM-1MZ

Analogue
compound: Heme
pdb: 2zawA
ligand het code: 6HE

Analogue
compound: (+)-exo-5-Hydroxycamphor
pdb: 1mpwA
ligand het code: TMH

Analogue
compound: (+)-exo-5-Hydroxycamphor
pdb: 1mpwB
ligand het code: TMH

Analogue
compound: (+)-exo-5-Hydroxycamphor
pdb: 8cppA
ligand het code: TCM

Analogue
pdb: 1pheA
ligand het code: SO4

Formation, crystal structure, and rearrangement of a cytochrome P-450cam iron-phenyl complex.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/2261467
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 29
pages: 8119-26
published year: 1990
authors:
  item: Raag R
  item: Swanson BA
  item: Poulos TL
  item: Ortiz de Montellano PR

Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/2001355
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 30
pages: 2674-84
published year: 1991
authors:
  item: Raag R
  item: Poulos TL

Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9675266
journal: Biochim Biophys Acta
volume: 1386
pages: 157-67
published year: 1998
authors:
  item: Aoki M
  item: Ishimori K
  item: Morishima I

Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11051557
journal: J Inorg Biochem
volume: 81
pages: 121-31
published year: 2000
authors:
  item: Das B
  item: Helms V
  item: Lounnas V
  item: Wade RC

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.16129

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.7590-7591

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.1, p.11426-11428

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.2680

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.1, Fig.3, p.677-678

ReferenceForCatalyticMechanism
reference index: 21
reference section: Fig.1, p.1179-1182

ReferenceForCatalyticMechanism
reference index: 25
reference section: Fig.10, p.1076

ReferenceForCatalyticMechanism
reference index: 30
reference section: p.9216-9218, Fig.10

ReferenceForCatalyticMechanism
reference index: 31
reference section: p.166

ReferenceForCatalyticMechanism
reference index: 32
reference section: Fig.1, p.176-177

ReferenceForCatalyticMechanism
reference index: 37
reference section: p.972-973, Fig.6

ReferenceForCatalyticMechanism
reference index: 40

ReferenceForCatalyticMechanism
reference index: 41
reference section: Fig.1, p.1617-1621

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 52
reference section: p.14512-14513

ReferenceForCatalyticMechanism
reference index: 54
reference section: Fig.4

ReferenceForCatalyticMechanism
reference index: 55
reference section: p.31662-31663

ReferenceForCatalyticMechanism
reference index: 58
reference section: Fig.1, p.508-514

ReferenceForCatalyticMechanism
reference index: 60
reference section: Scheme 1, p.477-479

ReferenceForCatalyticMechanism
reference index: 61
reference section: Fig.1, p.14136-14139

The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
medline id: 86059514
references: http://www.ncbi.nlm.nih.gov/pubmed/4066706
references: P00183
journal: J Biol Chem
volume: 260
pages: 16122-30
published year: 1985
authors:
  item: Poulos TL
  item: Finzel BC
  item: Gunsalus IC
  item: Wagner GC
  item: Kraut J

Crystal structure of substrate-free Pseudomonas putida cytochrome P-450.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3768350
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 25
pages: 5314-22
published year: 1986
authors:
  item: Poulos TL
  item: Finzel BC
  item: Howard AJ

P-450 binding to substrates camphor and linalool versus pressure.
type: BibliographicResource
comment: ABSORPTION SPECTROSCOPY
medline id: 87126838
references: http://www.ncbi.nlm.nih.gov/pubmed/3813557
references: P00183
journal: Arch Biochem Biophys
volume: 253
pages: 100-7
published year: 1987
authors:
  item: Marden MC
  item: Hoa GH

Crystal structures of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3442650
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 26
pages: 8165-74
published year: 1987
authors:
  item: Poulos TL
  item: Howard AJ

High-resolution crystal structure of cytochrome P450cam.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3656428
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 195
pages: 687-700
published year: 1987
authors:
  item: Poulos TL
  item: Finzel BC
  item: Howard AJ

Dynamic behavior of the active site structure in bacterial cytochrome P-450.
type: BibliographicResource
comment: FOURIER-TRANSFORM INFRARED SPECTROSCOPY
journal: Stud Biophys
volume: 120
pages: 241-51
published year: 1987
authors:
  item: Jung C
  item: Marlow F
references: P00183

Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure.
type: BibliographicResource
comment: ABSORPTION AND FLUORESCENCE SPECTROSCOPY
medline id: 89229061
references: http://www.ncbi.nlm.nih.gov/pubmed/2578028
references: P00183
journal: Biochemistry
volume: 28
pages: 651-6
published year: 1989
authors:
  item: Hui Bon Hoa G
  item: Di Primo C
  item: Dondaine I
  item: Sligar SG
  item: Gunsalus IC
  item: Douzou P

Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/2611203
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 28
pages: 7586-92
published year: 1989
authors:
  item: Raag R
  item: Poulos TL

The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/2713354
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 28
pages: 917-22
published year: 1989
authors:
  item: Raag R
  item: Poulos TL

Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/1742281
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 30
pages: 11420-9
published year: 1991
authors:
  item: Raag R
  item: Martinis SA
  item: Sligar SG
  item: Poulos TL

Structural and electronic characterization of heme moiety in oxygenated hemoproteins by using XANES spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1764462
journal: Biochim Biophys Acta
volume: 1115
pages: 101-7
published year: 1991
authors:
  item: Shiro Y
  item: Makino R
  item: Sato F
  item: Oyanagi H
  item: Matsushita T
  item: Ishimura Y
  item: Iizuka T

A 175-psec molecular dynamics simulation of camphor-bound cytochrome P-450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1749772
journal: Proteins
volume: 11
pages: 184-204
published year: 1991
authors:
  item: Paulsen MD
  item: Ornstein RL

Ethylbenzene hydroxylation by cytochrome P450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1449498
journal: Biochem Biophys Res Commun
volume: 189
pages: 488-95
published year: 1992
authors:
  item: Filipovic D
  item: Paulsen MD
  item: Loida PJ
  item: Sligar SG
  item: Ornstein RL

Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450.
type: BibliographicResource
comment: CIRCULAR DICHROISM SPECTROSCOPY
medline id: 92305023
references: http://www.ncbi.nlm.nih.gov/pubmed/1610873
references: P00183
journal: Biochim Biophys Acta
volume: 1100
pages: 171-6
published year: 1992
authors:
  item: Nolting B
  item: Jung C
  item: Snatzke G

Cytochrome P450cam: crystallography, oxygen activation, and electron transfer.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1537455
journal: FASEB J
volume: 6
pages: 674-9
published year: 1992
authors:
  item: Poulos TL
  item: Raag R

Inhibitor-induced conformational change in cytochrome P-450CAM.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8485133
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 32
pages: 4571-8
published year: 1993
authors:
  item: Raag R
  item: Li H
  item: Jones BC
  item: Poulos TL

Substrate mobility in thiocamphor-bound cytochrome P450cam: an explanation of the conflict between the observed product profile and the X-ray structure.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8332592
journal: Protein Eng
volume: 6
pages: 359-65
published year: 1993
authors:
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Effects of monovalent cations on cytochrome P-450 camphor. Evidence for preferential binding of potassium.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8034004
journal: FEBS Lett
volume: 347
pages: 207-10
published year: 1994
authors:
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Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8120894
journal: J Mol Biol
volume: 236
pages: 1169-85
published year: 1994
authors:
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  item: Ravichandran KG
  item: Peterson JA
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Comparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7700866
journal: Protein Eng
volume: 7
pages: 1345-51
published year: 1994
authors:
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Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: a molecular dynamics study.
type: BibliographicResource
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journal: Biophys J
volume: 69
pages: 810-24
published year: 1995
authors:
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Enzyme-catalyzed dehalogenation of pentachloroethane: why F87W-cytochrome P450cam is faster than wild type.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8637849
journal: Protein Eng
volume: 8
pages: 801-7
published year: 1995
authors:
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A three-dimensional model of aromatase cytochrome P450.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7549871
journal: Protein Sci
volume: 4
pages: 1065-80
published year: 1995
authors:
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1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton.
type: BibliographicResource
comment: STRUCTURE BY NMR
medline id: 97459726
references: http://www.ncbi.nlm.nih.gov/pubmed/9315686
references: P00183
journal: FEBS Lett
volume: 414
pages: 203-8
published year: 1997
authors:
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Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
medline id: 98019009
references: http://www.ncbi.nlm.nih.gov/pubmed/9357977
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journal: FEBS Lett
volume: 415
pages: 253-7
published year: 1997
authors:
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Identification of a functional water channel in cytochrome P450 enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9122160
journal: Proc Natl Acad Sci U S A
volume: 94
pages: 2133-8
published year: 1997
authors:
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An improved procedure for the preparation of X-ray diffraction-quality crystals of cytochrome p450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9761931
journal: Acta Crystallogr D Biol Crystallogr
volume: 54
pages: 470-2
published year: 1998
authors:
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Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
medline id: 98313255
references: http://www.ncbi.nlm.nih.gov/pubmed/9649301
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journal: Biochemistry
volume: 37
pages: 9211-9
published year: 1998
authors:
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NMR studies of putidaredoxin: associations of putidaredoxin with NADH-putidaredoxin reductase and cytochrome p450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9675270
journal: Biochim Biophys Acta
volume: 1386
pages: 168-78
published year: 1998
authors:
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Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
journal: J Am Chem Soc
volume: 120
pages: 46-52
published year: 1998
authors:
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Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9888815
journal: Biochemistry
volume: 38
pages: 751-61
published year: 1999
authors:
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Optical detection of cytochrome P450 by sensitizer-linked substrates.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS)
medline id: 20027486
references: http://www.ncbi.nlm.nih.gov/pubmed/10557259
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references: P00183
journal: Proc Natl Acad Sci U S A
volume: 96
pages: 12987-90
published year: 1999
authors:
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http://ezcatdb.cbrc.jp/EzCatDB/reference/S00033#36
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journal: Eur J Biochem
volume: 267
pages: 216-21
published year: 2000
authors:
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title: Assignment of heme methyl 1H-NMR resonances of high-spin and low-spin ferric complexes of cytochrome p450cam using one-dimensional and two-dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments.

X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS)
medline id: 21062556
references: http://www.ncbi.nlm.nih.gov/pubmed/11098139
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references: P00183
journal: J Biochem (Tokyo)
volume: 128
pages: 965-74
published year: 2000
authors:
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Enantiomeric discrimination of Ru-substrates by cytochrome P450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11051567
journal: J Inorg Biochem
volume: 81
pages: 221-8
published year: 2000
authors:
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Picture story. Freeze frame.
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references: http://www.ncbi.nlm.nih.gov/pubmed/10742167
journal: Nat Struct Biol
volume: 7
pages: 270
published year: 2000
authors:
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The catalytic pathway of cytochrome p450cam at atomic resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
medline id: 20165028
references: http://www.ncbi.nlm.nih.gov/pubmed/10698731
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journal: Science
volume: 287
pages: 1615-22
published year: 2000
authors:
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Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11583152
journal: Biochemistry
volume: 40
pages: 9532-8
published year: 2001
authors:
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Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
medline id: 21159060
references: http://www.ncbi.nlm.nih.gov/pubmed/11258878
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journal: Biochemistry
volume: 40
pages: 2669-77
published year: 2001
authors:
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A virtual high throughput screen for high affinity cytochrome P450cam substrates. Implications for in silico prediction of drug metabolism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11688945
journal: J Comput Aided Mol Des
volume: 15
pages: 649-57
published year: 2001
authors:
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Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS)
medline id: 21532932
references: http://www.ncbi.nlm.nih.gov/pubmed/11606730
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journal: Proc Natl Acad Sci U S A
volume: 98
pages: 12420-5
published year: 2001
authors:
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Fluorescent probes for cytochrome p450 structural characterization and inhibitor screening.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12197708
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journal: J Am Chem Soc
volume: 124
pages: 10254-5
published year: 2002
authors:
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Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/12114516
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journal: J Biol Chem
volume: 277
pages: 37519-26
published year: 2002
authors:
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Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin.
type: BibliographicResource
comment: SUBSTRATE-PROTEIN INTERACTION
medline id: 22222631
references: http://www.ncbi.nlm.nih.gov/pubmed/12237225
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journal: J Inorg Biochem
volume: 91
pages: 597-606
published year: 2002
authors:
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Impact of incorporating the 2C5 crystal structure into comparative models of cytochrome P450 2D6.
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references: http://www.ncbi.nlm.nih.gov/pubmed/12211002
journal: Proteins
volume: 49
pages: 216-31
published year: 2002
authors:
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Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes.
type: BibliographicResource
comment: X-ray crystallography
journal: Arch Biochem Biophys
volume: 409
pages: 25-31
published year: 2003
authors:
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Crystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/14556625
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journal: Biochemistry
volume: 42
pages: 11943-50
published year: 2003
authors:
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Infrared spectroscopic and mutational studies on putidaredoxin-induced conformational changes in ferrous CO-P450cam.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/14661963
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journal: Biochemistry
volume: 42
pages: 14507-14
published year: 2003
authors:
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  item: Egawa T
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  item: Park SY
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Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires.
type: BibliographicResource
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journal: J Mol Biol
volume: 344
pages: 455-69
published year: 2004
authors:
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Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15269210
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journal: J Biol Chem
volume: 279
pages: 42844-9
published year: 2004
authors:
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A survey of active site access channels in cytochromes P450.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15219983
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journal: J Inorg Biochem
volume: 98
pages: 1175-82
published year: 2004
authors:
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Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15858263
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Acta Crystallogr D Biol Crystallogr
volume: 61
pages: 539-44
published year: 2005
authors:
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Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15994329
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journal: J Biol Chem
volume: 280
pages: 31659-63
published year: 2005
authors:
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The status of high-valent metal oxo complexes in the P450 cytochromes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16510191
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journal: J Inorg Biochem
volume: 100
pages: 507-18
published year: 2006
authors:
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Cytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450(cam) by an L244A mutation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16943206
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journal: Protein Eng Des Sel
volume: 19
pages: 491-6
published year: 2006
authors:
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Structure-activity correlations in pentachlorobenzene oxidation by engineered cytochrome P450cam.
type: BibliographicResource
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journal: Protein Eng Des Sel
volume: 20
pages: 473-80
published year: 2007
authors:
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Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18001135
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journal: Biochemistry
volume: 46
pages: 14129-40
published year: 2007
authors:
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Evaluation of the functional role of the heme-6-propionate side chain in cytochrome P450cam.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/18088124
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Am Chem Soc
volume: 130
pages: 432-3
published year: 2008
authors:
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  item: Shimada H
  item: Hayashi T

camphor 5-monooxygenase
type: KeggEnzyme

camphor 5-exo-methylene hydroxylase
type: KeggEnzyme

2-bornanone 5-exo-hydroxylase
type: KeggEnzyme

bornanone 5-exo-hydroxylase
type: KeggEnzyme

camphor 5-exo-hydroxylase
type: KeggEnzyme

camphor 5-exohydroxylase
type: KeggEnzyme

camphor hydroxylase
type: KeggEnzyme

d-camphor monooxygenase
type: KeggEnzyme

methylene hydroxylase
type: KeggEnzyme

D-camphor-exo-hydroxylase
type: KeggEnzyme

camphor methylene hydroxylase
type: KeggEnzyme