M00039
type: Enzyme
active site residues resources: The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
active site residues resources: Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
active site residues resources: A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.
active site residues resources: P19921
active site residues resources: P19919
active site residues resources: P19920
cath: Ubiquitin-like (UB roll)
cath: DNA polymerase; domain 1
cath: Aldehyde Oxidoreductase; domain 3
cath: Aldehyde Oxidoreductase; domain 4
cath: Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
cath: Enolase-like; domain 1
cath: Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
csa: 1qj2
ec: https://purl.uniprot.org/enzyme/1.2.99.2
kegg cofactor: [2Fe-2S]
kegg cofactor: Dinuclear [Cu-S-Mo(=O)OH] cluster
kegg cofactor: Molybdopterin cytosine dinucleotide
kegg cofactor: FAD
kegg enzyme: carbon-monoxide dehydrogenase (acceptor)
kegg pathway: Trinitrotoluene degradation
kegg pathway: Methane metabolism
kegg product: CO2
kegg product: Reduced acceptor
kegg substrate: CO
kegg substrate: H2O
kegg substrate: Acceptor
macie: M0107
pdb: 1n5wA01
pdb: 1n5wD01
pdb: 1n60A01
pdb: 1n60D01
pdb: 1n61A01
pdb: 1n61D01
pdb: 1n62A01
pdb: 1n62D01
pdb: 1n63A01
pdb: 1n63D01
pdb: 1qj2A01
pdb: 1qj2G01
pdb: 1zxiA01
pdb: 1zxiD01
pdb: 1n5wA02
pdb: 1n5wD02
pdb: 1n60A02
pdb: 1n60D02
pdb: 1n61A02
pdb: 1n61D02
pdb: 1n62A02
pdb: 1n62D02
pdb: 1n63A02
pdb: 1n63D02
pdb: 1qj2A02
pdb: 1qj2G02
pdb: 1zxiA02
pdb: 1zxiD02
pdb: 1n5wB01
pdb: 1n5wE01
pdb: 1n60B01
pdb: 1n60E01
pdb: 1n61B01
pdb: 1n61E01
pdb: 1n62B01
pdb: 1n62E01
pdb: 1n63B01
pdb: 1n63E01
pdb: 1qj2B01
pdb: 1qj2H01
pdb: 1zxiB01
pdb: 1zxiE01
pdb: 1n5wB02
pdb: 1n5wE02
pdb: 1n60B02
pdb: 1n60E02
pdb: 1n61B02
pdb: 1n61E02
pdb: 1n62B02
pdb: 1n62E02
pdb: 1n63B02

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
ligand het code: OMO
pdb: 1n60B04

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
ligand het code: OMO
pdb: 1n60E04

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
ligand het code: CUB
pdb: 1n62B04

Analogue
compound: Dinuclear [Cu-S-Mo(=O)OH] cluster
ligand het code: CUB
pdb: 1n62E04

Analogue
compound: Molybdopterin cytosine dinucleotide
ligand het code: PCD
pdb: 1qj2B03

Analogue
compound: Molybdopterin cytosine dinucleotide
ligand het code: PCD
pdb: 1qj2H03

Analogue
compound: FAD
ligand het code: FAD
pdb: 1n5wC03

Analogue
compound: FAD
ligand het code: FAD
pdb: 1n5wF03

IntermediateAnalogue
ligand het code: CUB
pdb: 1n62B04

IntermediateAnalogue
ligand het code: CUB
pdb: 1n62E04

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.4, p.8887-8889

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.5, p.871-875

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.1224-1228

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.2, p.15974-15976

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig. 2, Fig. 6, Fig. 12, p.891-897

DNA polymerase; domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/1.10.150.120

Ubiquitin-like (UB roll)
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.10.20.30

Aldehyde Oxidoreductase; domain 4
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.30.365.10

Enolase-like; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.390.50

Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.43.10

Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.30.465.10

Aldehyde Oxidoreductase; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.1170.50

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

Trinitrotoluene degradation
type: KeggPathway
references: KEGG:MAP00633

Methane metabolism
type: KeggPathway
references: KEGG:MAP00680

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.
type: BibliographicResource
authors:
  item: Dobbek H
  item: Gremer L
  item: Meyer O
  item: Huber R
journal: Proc Natl Acad Sci U S A
medline id: 99362680
pages: 8884-9
published year: 1999
volume: 96
references: http://www.ncbi.nlm.nih.gov/pubmed/10430865
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P19919
references: P19920
references: P19921
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)

The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.
type: BibliographicResource
authors:
  item: Meyer O
  item: Gremer L
  item: Ferner R
  item: Ferner M
  item: Dobbek H
  item: Gnida M
  item: Meyer-Klaucke W
  item: Huber R
journal: Biol Chem
pages: 865-76
published year: 2000
volume: 381
references: http://www.ncbi.nlm.nih.gov/pubmed/11076018

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00039#3
type: BibliographicResource
title: Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli.
authors:
  item: Gremer L
  item: Kellner S
  item: Dobbek H
  item: Huber R
  item: Meyer O
journal: J Biol Chem
pages: 1864-72
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/10636886

Quantum chemical modeling of CO oxidation by the active site of molybdenum CO dehydrogenase.
type: BibliographicResource
authors:
  item: Siegbahn PE
  item: Shestakov AF
journal: J Comput Chem
pages: 888-98
published year: 2005
volume: 26
references: http://www.ncbi.nlm.nih.gov/pubmed/15834924

Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans.
type: BibliographicResource
authors:
  item: Resch M
  item: Dobbek H
  item: Meyer O
journal: J Biol Inorg Chem
pages: 518-28
published year: 2005
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/16091936
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
type: BibliographicResource
authors:
  item: Hanzelmann P
  item: Dobbek H
  item: Gremer L
  item: Huber R
  item: Meyer O
journal: J Mol Biol
pages: 1221-35
published year: 2000
volume: 301
references: http://www.ncbi.nlm.nih.gov/pubmed/10966817

Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
type: BibliographicResource
authors:
  item: Dobbek H
  item: Gremer L
  item: Kiefersauer R
  item: Huber R
  item: Meyer O
journal: Proc Natl Acad Sci U S A
medline id: 22364130
pages: 15971-6
published year: 2002
volume: 99
references: http://www.ncbi.nlm.nih.gov/pubmed/12475995
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P19919
references: P19920
references: P19921
comment: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).

A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.
type: BibliographicResource
authors:
  item: Gnida M
  item: Ferner R
  item: Gremer L
  item: Meyer O
  item: Meyer-Klaucke W
journal: Biochemistry
pages: 222-30
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/12515558

1n5wA01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n5wA02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n5wB04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n5wD01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n5wD02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n5wE04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n60A01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n60A02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n60D01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n60D02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n61A01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n61A02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n61B04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n61D01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n61D02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n61E04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n62A01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n62A02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n62D01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n62D02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n63A01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1n63A02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1n63B04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1n63D01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1n63D02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1n63E04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1qj2A01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1qj2A02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1qj2G01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1qj2G02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1zxiA01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1zxiA02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1zxiB04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1zxiD01
type: Pdb
cofactor binding residue: CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1zxiD02
type: Pdb
cofactor binding residue: CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1zxiE04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1n5wB05
type: Pdb
catalytic residue: GLN 240
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n5wE05
type: Pdb
catalytic residue: GLN 240
references: 1n5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n5w

1n60B04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n60B05
type: Pdb
catalytic residue: GLN 240
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n60E04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n60E05
type: Pdb
catalytic residue: GLN 240
references: 1n60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n60

1n61B05
type: Pdb
catalytic residue: GLN 240
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n61E05
type: Pdb
catalytic residue: GLN 240
references: 1n61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n61

1n62B04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n62B05
type: Pdb
catalytic residue: GLN 240
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n62E04
type: Pdb
catalytic residue: CYS 388;GLU 763
cofactor binding residue: CYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n62E05
type: Pdb
catalytic residue: GLN 240
references: 1n62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n62

1n63B05
type: Pdb
catalytic residue: GLN 240
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1n63E05
type: Pdb
catalytic residue: GLN 240
references: 1n63
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1n63

1qj2B04
type: Pdb
catalytic residue: ;GLU 763
cofactor binding residue: EYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
modified residue: EYS 388(Selanylated)
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1qj2B05
type: Pdb
catalytic residue: GLN 240
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1qj2H04
type: Pdb
catalytic residue: ;GLU 763
cofactor binding residue: EYS 388(Copper binding);GLU 763(Molybdenum binding)
main chain in catalysis: ARG 387
modified residue: EYS 388(Selanylated)
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1qj2H05
type: Pdb
catalytic residue: GLN 240
references: 1qj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qj2

1zxiB05
type: Pdb
catalytic residue: GLN 240
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

1zxiE05
type: Pdb
catalytic residue: GLN 240
references: 1zxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zxi

[2Fe-2S]
type: KeggCofactor
compound type: heavy metal
compound type: sulfide group
references: KEGG:L00023
references: CHEBI:33739

FAD
type: KeggCofactor
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
references: KEGG:C00016
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Molybdopterin cytosine dinucleotide
type: KeggCofactor
compound type: amide group
compound type: amine group
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
compound type: sulfhydryl group
references: KEGG:L00006
references: CHEBI:43955
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Dinuclear [Cu-S-Mo(=O)OH] cluster
type: KeggCofactor
compound type: heavy metal
compound type: sulfide group
references: KEGG:C99999

CO2
type: KeggProduct
compound type: others
references: KEGG:C00011
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Acceptor
type: KeggSubstrate
compound type: others
references: KEGG:C00028

Reduced acceptor
type: KeggProduct
compound type: others
references: KEGG:C00030

CO
type: KeggSubstrate
compound type: others
references: KEGG:C00237
references: CHEBI:17245
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

anaerobic carbon monoxide dehydrogenase
type: KeggEnzyme

carbon monoxide oxygenase
type: KeggEnzyme

carbon-monoxide dehydrogenase
type: KeggEnzyme

carbon-monoxide:(acceptor) oxidoreductase
type: KeggEnzyme