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Ligands
Code Name Style Show Link
CU Copper (II) ion
CUM Cu(I)-S-mo(VI)(=O)oh cluster
FAD Flavin-adenine dinucleotide
FES Fe2/s2 (inorganic) cluster
MCN Pterin cytosine dinucleotide
PO4 Phosphate ion
Non-standard Residues
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Code : 1ZXI   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Reconstituted CO dehydrogenase from Oligotropha carboxidovorans
Release Data : 2005-10-11
Compound :
mol_id molecule chains synonym
1 Carbon monoxide dehydrogenase small chain A,D CO dehydrogenase subunit S, CO-DH S
ec: 1.2.99.2
mol_id molecule chains synonym
2 Carbon monoxide dehydrogenase large chain B,E CO dehydrogenase subunit L, CO-DH L
ec: 1.2.99.2
mol_id molecule chains synonym
3 Carbon monoxide dehydrogenase medium chain C,F CO dehydrogenase subunit M, CO-DH M
ec: 1.2.99.2
Source :
mol_id organism_scientific
1 Oligotropha carboxidovorans  (taxid:504832)
strain: OM5
mol_id organism_scientific
2 Oligotropha carboxidovorans  (taxid:504832)
strain: OM5
mol_id organism_scientific
3 Oligotropha carboxidovorans  (taxid:504832)
strain: OM5
Authors : Resch, M., Dobbek, H., Meyer, O.
Keywords : Molybdoprotein, CODH, Molybdenum, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.7 Å )
Citation :

Structural and functional reconstruction in situ of the [CuSMoO(2)] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans

Resch, M.,Dobbek, H.,Meyer, O.
(2005)  J.Biol.Inorg.Chem.  10 : 518 - 528

PubMed: 16091936
DOI: 10.1007/s00775-005-0006-4

Chain : A, D
UniProt : P19921 (DCMS_AFIC5)
Reaction: EC: Evidence:
Physiological Direction:
a quinone + CO + H2O = a quinol + CO2 1.2.5.3 PubMed:12475995, PubMed:21275368
-
Chain : B, E
UniProt : P19919 (DCML_AFIC5)
Reaction: EC: Evidence:
Physiological Direction:
a quinone + CO + H2O = a quinol + CO2 1.2.5.3 PubMed:12475995, PubMed:21275368
-
Chain : C, F
UniProt : P19920 (DCMM_AFIC5)
Reaction: EC: Evidence:
Physiological Direction:
a quinone + CO + H2O = a quinol + CO2 1.2.5.3 PubMed:12475995, PubMed:21275368
-