D00265
type: Enzyme
active site residues resources: Structure, evolution and action of vitamin B6-dependent enzymes.
active site residues resources: Mechanisms to account for maintenance of the soluble methionine pool in transgenic Arabidopsis plants expressing antisense cystathionine gamma-synthase cDNA.
active site residues resources: Identification of a short highly conserved amino acid sequence as the functional region required for posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis.
cath: Aspartate Aminotransferase; domain 2
cath: Aspartate Aminotransferase, domain 1
csa: 1cs1
csa: 1qgn
ec: https://purl.uniprot.org/enzyme/2.5.1.48
kegg cofactor: Pyridoxal phosphate
kegg enzyme: cystathionine gamma-synthase
kegg pathway: Methionine metabolism
kegg pathway: Cysteine metabolism
kegg pathway: Selenoamino acid metabolism
kegg pathway: Sulfur metabolism
kegg product: Cystathionine
kegg product: Succinate
kegg substrate: O-Succinyl-L-homoserine
kegg substrate: L-Cysteine
pdb: 1cs1A01
pdb: 1cs1B01
pdb: 1cs1C01
pdb: 1cs1D01
pdb: 1qgnA01
pdb: 1qgnB01
pdb: 1qgnC01
pdb: 1qgnD01
pdb: 1qgnE01
pdb: 1qgnF01
pdb: 1qgnG01
pdb: 1qgnH01
pdb: 1i41A01
pdb: 1i41B01
pdb: 1i41C01
pdb: 1i41D01
pdb: 1i41E01
pdb: 1i41F01
pdb: 1i41G01
pdb: 1i41H01
pdb: 1i41I01
pdb: 1i41J01
pdb: 1i41K01
pdb: 1i41L01
pdb: 1i43A01
pdb: 1i43B01
pdb: 1i43C01
pdb: 1i43D01
pdb: 1i43E01
pdb: 1i43F01
pdb: 1i43G01
pdb: 1i43H01
pdb: 1i43I01
pdb: 1i43J01
pdb: 1i43K01
pdb: 1i43L01
pdb: 1i48A01
pdb: 1i48B01
pdb: 1i48C01
pdb: 1i48D01
pdb: 1i48E01
pdb: 1i48F01
pdb: 1i48G01
pdb: 1i48H01
pdb: 1i48I01
pdb: 1i48J01
pdb: 1i48K01
pdb: 1i48L01
pdb: 1cs1A02
pdb: 1cs1B02
pdb: 1cs1C02
pdb: 1cs1D02
pdb: 1qgnA02
pdb: 1qgnB02
pdb: 1qgnC02
pdb: 1qgnD02
pdb: 1qgnE02
pdb: 1qgnF02
pdb: 1qgnG02
pdb: 1qgnH02
pdb: 1i41A02

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41A01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41B01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41C01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41D01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41E01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41F01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41G01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41H01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41I01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41J01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41K01

Analogue
compound: Pyridoxal phosphate
ligand het code: HEN
pdb: 1i41L01

Analogue
compound: Succinate
ligand het code: DHD
pdb: 1cs1D01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41A01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41B01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41C01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41D01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41E01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41F01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41G01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41H01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41I01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41J01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41K01

IntermediateAnalogue
ligand het code: HEN
pdb: 1i41L01

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.7, p.6834-6839
reference step: 9

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.7, p.987-990, p.992-994
reference step: 8

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.797

Aspartate Aminotransferase; domain 2
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.640.10

Aspartate Aminotransferase, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.1150.10

Methionine metabolism
type: KeggPathway
references: KEGG:MAP00271

Cysteine metabolism
type: KeggPathway
references: KEGG:MAP00272

Selenoamino acid metabolism
type: KeggPathway
references: KEGG:MAP00450

Sulfur metabolism
type: KeggPathway
references: KEGG:MAP00920

Proton retention in the gamma-elimination reaction catalysed by cystathionine gamma-synthase.
type: BibliographicResource
authors:
  item: Guggenheim S
  item: Flavin M
journal: Biochim Biophys Acta
pages: 664-9
published year: 1968
volume: 151
references: http://www.ncbi.nlm.nih.gov/pubmed/5646044

Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor.
type: BibliographicResource
authors:
  item: Steegborn C
  item: Laber B
  item: Messerschmidt A
  item: Huber R
  item: Clausen T
journal: J Mol Biol
pages: 789-801
published year: 2001
volume: 311
references: http://www.ncbi.nlm.nih.gov/pubmed/11518531
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Homocysteine biosynthesis in green plants. O-Phosphorylhomoserine as the physiological substrate for cystathionine gamma-synthase.
type: BibliographicResource
authors:
  item: Datko AH
  item: Giovanelli J
  item: Mudd SH
journal: J Biol Chem
pages: 1139-55
published year: 1974
volume: 249
references: http://www.ncbi.nlm.nih.gov/pubmed/4205315

Cloning, purification, crystallization, and preliminary X-ray diffraction analysis of cystathionine gamma-synthase from E. coli.
type: BibliographicResource
authors:
  item: Wahl MC
  item: Huber R
  item: Prade L
  item: Marinkovic S
  item: Messerschmidt A
  item: Clausen T
journal: FEBS Lett
pages: 492-6
published year: 1997
volume: 414
references: http://www.ncbi.nlm.nih.gov/pubmed/9323022

Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution.
type: BibliographicResource
authors:
  item: Clausen T
  item: Huber R
  item: Prade L
  item: Wahl MC
  item: Messerschmidt A
journal: EMBO J
medline id: 99059720
pages: 6827-38
published year: 1998
volume: 17
references: http://www.ncbi.nlm.nih.gov/pubmed/9843488
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00935
comment: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)

Cloning, purification and characterisation of cystathionine gamma-synthase from Nicotiana tabacum.
type: BibliographicResource
authors:
  item: Clausen T
  item: Wahl MC
  item: Messerschmidt A
  item: Huber R
  item: Fuhrmann JC
  item: Laber B
  item: Streber W
  item: Steegborn C
journal: Biol Chem
pages: 1237-42
published year: 1999
volume: 380
references: http://www.ncbi.nlm.nih.gov/pubmed/10595588

The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity.
type: BibliographicResource
authors:
  item: Steegborn C
  item: Messerschmidt A
  item: Laber B
  item: Streber W
  item: Huber R
  item: Clausen T
journal: J Mol Biol
pages: 983-96
published year: 1999
volume: 290
references: http://www.ncbi.nlm.nih.gov/pubmed/10438597
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The manifold of vitamin B6 dependent enzymes.
type: BibliographicResource
authors:
  item: Schneider G
  item: Kack H
  item: Lindqvist Y
journal: Structure Fold Des
pages: R1-6
published year: 2000
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10673430

Identification of a short highly conserved amino acid sequence as the functional region required for posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis.
type: BibliographicResource
authors:
  item: Ominato K
  item: Akita H
  item: Suzuki A
  item: Kijima F
  item: Yoshino T
  item: Yoshino M
  item: Chiba Y
  item: Onouchi H
  item: Naito S
journal: J Biol Chem
pages: 36380-6
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/12121993

Structure, evolution and action of vitamin B6-dependent enzymes.
type: BibliographicResource
authors:
  item: Jansonius JN
journal: Curr Opin Struct Biol
pages: 759-69
published year: 1998
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/9914259

Mechanisms to account for maintenance of the soluble methionine pool in transgenic Arabidopsis plants expressing antisense cystathionine gamma-synthase cDNA.
type: BibliographicResource
authors:
  item: Gakiere B
  item: Ravanel S
  item: Droux M
  item: Douce R
  item: Job D
journal: C R Acad Sci III
pages: 841-51
published year: 2000
volume: 323
references: http://www.ncbi.nlm.nih.gov/pubmed/11098400

1cs1A01
type: Pdb
catalytic residue: TYR 46;ARG 48;TYR 101;ASP 173;LLP 198
modified residue: LLP 198(Modified by PLP)
references: 1cs1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cs1

1cs1B01
type: Pdb
catalytic residue: TYR 46;ARG 48;TYR 101;ASP 173;LLP 198
modified residue: LLP 198(Modified by PLP)
references: 1cs1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cs1

1cs1C01
type: Pdb
catalytic residue: TYR 46;ARG 48;TYR 101;ASP 173;LLP 198
modified residue: LLP 198(Modified by PLP)
references: 1cs1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cs1

1cs1D01
type: Pdb
catalytic residue: TYR 46;ARG 48;TYR 101;ASP 173;LLP 198
modified residue: LLP 198(Modified by PLP)
references: 1cs1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cs1

1i43A01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43B01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43C01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43D01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43E01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43F01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43G01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43H01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43I01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43J01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43K01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i43L01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i43
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i43

1i48A01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48B01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48C01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48D01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48E01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48F01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48G01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48H01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48I01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48J01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48K01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1i48L01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i48
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i48

1qgnA01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnB01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnC01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnD01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnE01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnF01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnG01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1qgnH01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1qgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qgn

1i41A01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41B01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41C01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41D01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41E01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41F01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41G01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41H01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41I01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41J01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41K01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

1i41L01
type: Pdb
catalytic residue: TYR 108;ARG 110;TYR 163;ASP 236;LYS 261
cofactor binding residue: LYS 261(PLP binding)
references: 1i41
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i41

Pyridoxal phosphate
type: KeggCofactor
compound type: aromatic ring (with nitrogen atoms)
compound type: phosphate group/phosphate ion
references: KEGG:C00018
references: CHEBI:18405
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Succinate
type: KeggProduct
compound type: carboxyl group
references: KEGG:C00042
references: CHEBI:15741
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Cysteine
type: KeggSubstrate
compound type: amino acids
compound type: sulfhydryl group
references: KEGG:C00097
references: CHEBI:17561
references: CHEBI:35235
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Cystathionine
type: KeggProduct
compound type: amino acids
compound type: sulfide group
references: KEGG:C00542
references: CHEBI:17755
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

O-Succinyl-L-homoserine
type: KeggSubstrate
compound type: amino acids
compound type: carbohydrate
compound type: carboxyl group
references: KEGG:C01118
references: CHEBI:16160
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

O-succinyl-L-homoserine succinate-lyase (adding cysteine)
type: KeggEnzyme

O-succinylhomoserine (thiol)-lyase
type: KeggEnzyme

homoserine O-transsuccinylase
type: KeggEnzyme

O-succinylhomoserine synthase
type: KeggEnzyme

O-succinylhomoserine synthetase
type: KeggEnzyme

cystathionine synthase
type: KeggEnzyme

cystathionine synthetase
type: KeggEnzyme

homoserine transsuccinylase
type: KeggEnzyme

4-O-succinyl-L-homoserine:L-cysteineS-(3-amino-3-carboxypropyl)transferase
type: KeggEnzyme