M00317
type: Enzyme
active site residues resources: Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding.
active site residues resources: P00751
cath: Rossmann fold
cath: Thrombin, subunit H
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/2.-.-.-
cath: Immunoglobulin-like
cath: Jelly Rolls
cath: Glycosyltransferase
cath: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
ec: https://purl.uniprot.org/enzyme/3.4.21.47
kegg cofactor: Magnesium
kegg enzyme: Alternative-complement-pathway C3/C5 convertase
kegg intermediate: Peptidyl-tetrahedral intermediate
kegg intermediate: Acyl-enzyme
kegg intermediate: tetrahedral intermediate
kegg product: Complement component C3a
kegg product: Complement component C3b
kegg product: Complement component C5a
kegg product: Complement component C5b
kegg substrate: Complement C3 alpha chain
kegg substrate: Complement C5 alpha chain
kegg substrate: H2O
pdb: 1q0pA00
pdb: 1rrkA01
pdb: 1rs0A01
pdb: 1rtkA01
pdb: 2ok5A04
pdb: 2winI01
pdb: 2winJ01
pdb: 2winK01
pdb: 2winL01
pdb: 2xwbF04
pdb: 2xwbH04
pdb: 2xwjI04
pdb: 2xwjJ04
pdb: 2xwjK04
pdb: 2xwjL04
pdb: 3hrzD04
pdb: 3hs0D04
pdb: 3hs0I04
pdb: 1rrkA02
pdb: 1rs0A02
pdb: 1rtkA02
pdb: 1dleA01
pdb: 1dleB01
pdb: 2ok5A05
pdb: 2winI02
pdb: 2winJ02
pdb: 2winK02
pdb: 2winL02
pdb: 2xwbF05
pdb: 2xwbH05
pdb: 2xwjI05
pdb: 2xwjJ05
pdb: 2xwjK05
pdb: 2xwjL05
pdb: 3hrzD05
pdb: 3hs0D05
pdb: 3hs0I05
pdb: 1rrkA03
pdb: 1rs0A03
pdb: 1rtkA03
pdb: 1dleA02
pdb: 1dleB02
pdb: 2ok5A06
pdb: 2winI03
pdb: 2winJ03
pdb: 2winK03
pdb: 2winL03
pdb: 2xwbF06
pdb: 2xwbH06
pdb: 2xwjI06
pdb: 2xwjJ06
pdb: 2xwjK06
pdb: 2xwjL06
pdb: 3hrzD06
pdb: 3hs0D06
pdb: 3hs0I06
pdb: 2winB01

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1q0pA00

Analogue
compound: Magnesium
ligand het code: _CO
pdb: 1rrkA01

Analogue
compound: Magnesium
ligand het code: _NI
pdb: 2xwjI04

Analogue
compound: Magnesium
ligand het code: _NI
pdb: 2xwjJ04

Analogue
compound: Magnesium
ligand het code: _NI
pdb: 2xwjK04

Analogue
compound: Magnesium
ligand het code: _NI
pdb: 2xwjL04

TransitionStateAnalogue
compound: Peptidyl-tetrahedral intermediate
ligand het code: DFP
pdb: 1rs0A03

IntermediateAnalogue
compound: Acyl-enzyme
ligand het code: GBS
pdb: 1rtkA03

ReferenceForCatalyticMechanism
reference index: 16
reference section: Figure 5

ReferenceForCatalyticMechanism
reference index: 17
reference section: Figure 1

ReferenceForCatalyticMechanism
reference index: 20
reference section: Figure 1

ReferenceForCatalyticMechanism
reference index: 21
reference section: Figure 3

ReferenceForCatalyticMechanism
reference index: 22
reference section: Figure 6

Glycosyltransferase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.50.10.20

Thrombin, subunit H
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.40.10.10

OB fold (Dihydrolipoamide Acetyltransferase, E2P)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.50.120

Jelly Rolls
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.120.290

Immunoglobulin-like
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.40.690

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.410

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

Characterization of the initial C3 convertase of the alternative pathway of human complement.
type: BibliographicResource
authors:
  item: Fishelson Z
  item: Pangburn MK
  item: Muller-Eberhard HJ
journal: J Immunol
pages: 1430-4
published year: 1984
volume: 132
references: http://www.ncbi.nlm.nih.gov/pubmed/6559201

Functional role of the noncatalytic subunit of complement C5 convertase.
type: BibliographicResource
authors:
  item: Rawal N
  item: Pangburn MK
journal: J Immunol
pages: 1379-85
published year: 2000
volume: 164
references: http://www.ncbi.nlm.nih.gov/pubmed/10640753

Conformational changes during the assembly of factor B from its domains by (1)H NMR spectroscopy and molecular modelling: their relevance to the regulation of factor B activity.
type: BibliographicResource
authors:
  item: Hinshelwood J
  item: Perkins SJ
journal: J Mol Biol
pages: 1267-85
published year: 2000
volume: 301
references: http://www.ncbi.nlm.nih.gov/pubmed/10966820

Structural biology of the alternative pathway convertase.
type: BibliographicResource
authors:
  item: Xu Y
  item: Narayana SV
  item: Volanakis JE
journal: Immunol Rev
pages: 123-35
published year: 2001
volume: 180
references: http://www.ncbi.nlm.nih.gov/pubmed/11414354

Structure/function of C5 convertases of complement.
type: BibliographicResource
authors:
  item: Rawal N
  item: Pangburn MK
journal: Int Immunopharmacol
pages: 415-22
published year: 2001
volume: 1
references: http://www.ncbi.nlm.nih.gov/pubmed/11367526

Formation of high-affinity C5 convertases of the alternative pathway of complement.
type: BibliographicResource
authors:
  item: Rawal N
  item: Pangburn M
journal: J Immunol
pages: 2635-42
published year: 2001
volume: 166
references: http://www.ncbi.nlm.nih.gov/pubmed/11160326

Structure and function of complement C5 convertase enzymes.
type: BibliographicResource
authors:
  item: Pangburn MK
  item: Rawal N
journal: Biochem Soc Trans
pages: 1006-10
published year: 2002
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/12440962

Serine protease mechanism and specificity.
type: BibliographicResource
authors:
  item: Hedstrom L
journal: Chem Rev
pages: 4501-24
published year: 2002
volume: 102
references: http://www.ncbi.nlm.nih.gov/pubmed/12475199

Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase.
type: BibliographicResource
authors:
  item: Ponnuraj K
  item: Xu Y
  item: Macon K
  item: Moore D
  item: Volanakis JE
  item: Narayana SV
journal: Mol Cell
pages: 17-28
published year: 2004
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/15068800
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00751

Crystal structure of the A domain from complement factor B reveals an integrin-like open conformation.
type: BibliographicResource
authors:
  item: Bhattacharya AA
  item: Lupher ML Jr
  item: Staunton DE
  item: Liddington RC
journal: Structure
pages: 371-8
published year: 2004
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/15016353
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00751

The role of properdin in the assembly of the alternative pathway C3 convertases of complement.
type: BibliographicResource
authors:
  item: Hourcade DE
journal: J Biol Chem
pages: 2128-32
published year: 2006
volume: 281
references: http://www.ncbi.nlm.nih.gov/pubmed/16301317

The C3 convertase of the alternative pathway of human complement. Enzymic properties of the bimolecular proteinase.
type: BibliographicResource
authors:
  item: Pangburn MK
  item: Muller-Eberhard HJ
journal: Biochem J
pages: 723-30
published year: 1986
volume: 235
references: http://www.ncbi.nlm.nih.gov/pubmed/3638964

Factor B structure provides insights into activation of the central protease of the complement system.
type: BibliographicResource
authors:
  item: Milder FJ
  item: Gros P
  item: Gomes L
  item: Schouten A
  item: Janssen BJ
  item: Huizinga EG
  item: Romijn RA
  item: Hemrika W
  item: Roos A
  item: Daha MR
journal: Nat Struct Mol Biol
pages: 224-8
published year: 2007
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/17310251
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00751

Complement driven by conformational changes.
type: BibliographicResource
authors:
  item: Gros P
  item: Milder FJ
  item: Janssen BJ
journal: Nat Rev Immunol
pages: 48-58
published year: 2008
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/18064050

Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
type: BibliographicResource
authors:
  item: Janssen BJ
  item: Gomes L
  item: Koning RI
  item: Svergun DI
  item: Koster AJ
  item: Fritzinger DC
  item: Vogel CW
  item: Gros P
journal: EMBO J
pages: 2469-78
published year: 2009
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/19574954
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00751
references: Q91132

Coexistence of closed and open conformations of complement factor B in the alternative pathway C3bB(Mg2+) proconvertase.
type: BibliographicResource
authors:
  item: Torreira E
  item: Tortajada A
  item: Montes T
  item: Rodriguez de Cordoba S
  item: Llorca O
journal: J Immunol
pages: 7347-51
published year: 2009
volume: 183
references: http://www.ncbi.nlm.nih.gov/pubmed/19890040

Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor.
type: BibliographicResource
authors:
  item: Rooijakkers SH
  item: van Strijp JA
  item: Gros P
  item: Wu J
  item: Ruyken M
  item: van Domselaar R
  item: Planken KL
  item: Tzekou A
  item: Ricklin D
  item: Lambris JD
  item: Janssen BJ
journal: Nat Immunol
pages: 721-7
published year: 2009
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/19503103
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00751
references: P01024

3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase.
type: BibliographicResource
authors:
  item: Torreira E
  item: Tortajada A
  item: Montes T
  item: Rodriguez de Cordoba S
  item: Llorca O
journal: Proc Natl Acad Sci U S A
pages: 882-7
published year: 2009
volume: 106
references: http://www.ncbi.nlm.nih.gov/pubmed/19136636

Structures of C3b in complex with factors B and D give insight into complement convertase formation.
type: BibliographicResource
authors:
  item: Forneris F
  item: Ricklin D
  item: Wu J
  item: Tzekou A
  item: Wallace RS
  item: Lambris JD
  item: Gros P
journal: Science
pages: 1816-20
published year: 2010
volume: 330
references: http://www.ncbi.nlm.nih.gov/pubmed/21205667
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Alternative complement pathway activation fragment Ba binds to C3b. Evidence that formation of the factor B-C3b complex involves two discrete points of contact.
type: BibliographicResource
authors:
  item: Pryzdial EL
  item: Isenman DE
journal: J Biol Chem
pages: 1519-25
published year: 1987
volume: 262
references: http://www.ncbi.nlm.nih.gov/pubmed/3643213

Probing functional sites on complement protein B with monoclonal antibodies. Evidence for C3b-binding sites on Ba.
type: BibliographicResource
authors:
  item: Ueda A
  item: Kearney JF
  item: Roux KH
  item: Volanakis JE
journal: J Immunol
pages: 1143-9
published year: 1987
volume: 138
references: http://www.ncbi.nlm.nih.gov/pubmed/2433342

C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme.
type: BibliographicResource
authors:
  item: Kinoshita T
  item: Takata Y
  item: Kozono H
  item: Takeda J
  item: Hong KS
  item: Inoue K
journal: J Immunol
pages: 3895-901
published year: 1988
volume: 141
references: http://www.ncbi.nlm.nih.gov/pubmed/3183384

Analysis of the short consensus repeats of human complement factor B by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Hourcade DE
  item: Wagner LM
  item: Oglesby TJ
journal: J Biol Chem
pages: 19716-22
published year: 1995
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/7649982

C5 convertase of the alternative pathway of complement. Kinetic analysis of the free and surface-bound forms of the enzyme.
type: BibliographicResource
authors:
  item: Rawal N
  item: Pangburn MK
journal: J Biol Chem
pages: 16828-35
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9642242

New structural motifs on the chymotrypsin fold and their potential roles in complement factor B.
type: BibliographicResource
authors:
  item: Jing H
  item: Xu Y
  item: Carson M
  item: Moore D
  item: Macon KJ
  item: Volanakis JE
  item: Narayana SV
journal: EMBO J
pages: 164-73
published year: 2000
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/10637221
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00751
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 467-764.

Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding.
type: BibliographicResource
authors:
  item: Xu Y
  item: Circolo A
  item: Jing H
  item: Wang Y
  item: Narayana SV
  item: Volanakis JE
journal: J Biol Chem
pages: 378-85
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/10617628

1rs0A01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 1rs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rs0

1rtkA01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 1rtk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rtk

2winI01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winJ01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winK01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winL01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2xwbF04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwbH04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

3hrzD04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 3hrz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hrz

3hs0D04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 3hs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hs0

3hs0I04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 3hs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hs0

1dleA01
type: Pdb
catalytic residue: HIS 57;ASP 102
references: 1dle
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dle

1dleA02
type: Pdb
catalytic residue: SER 195
main chain in catalysis: GLY 193;SER 195
references: 1dle
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dle

1dleB01
type: Pdb
catalytic residue: HIS 57;ASP 102
references: 1dle
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dle

1dleB02
type: Pdb
catalytic residue: SER 195
main chain in catalysis: GLY 193;SER 195
references: 1dle
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dle

1q0pA00
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 1q0p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1q0p

1rrkA01
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 1rrk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rrk

1rrkA02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 1rrk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rrk

1rrkA03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 1rrk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rrk

1rs0A02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 1rs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rs0

1rs0A03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 1rs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rs0

1rtkA02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 1rtk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rtk

1rtkA03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 1rtk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rtk

2ok5A04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2ok5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ok5

2ok5A05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2ok5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ok5

2ok5A06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2ok5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ok5

2winB06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winD06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winF06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winH06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winI02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winI03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winJ02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winJ03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winK02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winK03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winL02
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2winL03
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2win
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2win

2xwbB06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwbD06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwbF05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwbF06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwbH05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwbH06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2xwb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwb

2xwjB06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjD06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjF06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjH06
type: Pdb
cofactor binding residue: ASN 1641(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjI04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjI05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjI06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjJ04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjJ05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjJ06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjK04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjK05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjK06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjL04
type: Pdb
cofactor binding residue: SER 253;SER 255;THR 328(Magnesium binding)
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjL05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

2xwjL06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 2xwj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2xwj

3hrzC03
type: Pdb
cofactor binding residue: THR 1620(Magnesium binding)
references: 3hrz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hrz

3hrzD05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 3hrz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hrz

3hrzD06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 3hrz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hrz

3hs0D05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 3hs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hs0

3hs0D06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 3hs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hs0

3hs0I05
type: Pdb
catalytic residue: HIS 501;ASP 551
references: 3hs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hs0

3hs0I06
type: Pdb
catalytic residue: SER 674
main chain in catalysis: GLY 672;SER 674
references: 3hs0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hs0

Magnesium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Acyl-enzyme
type: KeggIntermediate
references: KEGG:I00085

tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00086

Peptidyl-tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00087

Complement component C3b
type: KeggProduct
compound type: peptide/protein
references: KEGG:L00079

Complement C3 alpha chain
type: KeggSubstrate
compound type: peptide/protein
references: KEGG:L00091

Complement C5 alpha chain
type: KeggSubstrate
compound type: peptide/protein
references: KEGG:L00092

Complement component C3a
type: KeggProduct
compound type: peptide/protein
references: KEGG:L00093

Complement component C5a
type: KeggProduct
compound type: peptide/protein
references: KEGG:L00094

Complement component C5b
type: KeggProduct
compound type: peptide/protein
references: KEGG:L00095

Complement component C3/C5 convertase (alternative)
type: KeggEnzyme

Proenzyme factor B
type: KeggEnzyme

Properdin factor B
type: KeggEnzyme

C3 proactivator
type: KeggEnzyme

Glycine-rich beta-glycoprotein
type: KeggEnzyme

Heat-labile factor
type: KeggEnzyme

C3 convertase
type: KeggEnzyme

C3b,Bb,CVF,Bb,C5 convertase
type: KeggEnzyme

(C3b)n,Bb
type: KeggEnzyme

Complement C 3(C 5) convertase (amplification)
type: KeggEnzyme

Alternative complement pathway C3(C5) convertase
type: KeggEnzyme

C5 convertase
type: KeggEnzyme

CVF,Bb
type: KeggEnzyme

(CVF)-dependent glycine-rich-beta-glucoprotein
type: KeggEnzyme

Cobra venom factor-dependent C3 convertase
type: KeggEnzyme