Structure of PDB 1oao Chain B

Receptor sequence
>1oaoB (length=673) Species: 1525 (Moorella thermoacetica) [Search protein sequence]
PRFRDLSHNCRPSEAPRVMEPKNRDRTVDPAVLEMLVKSKDDKVITAFDR
FVAQQPQCKIGYEGICCRFCMAGPCRIKATDGPGSRGICGASAWTIVARN
VGLMILTGAAAHCEHGNHIAHALVEMAEGKAPDYSVKDEAKLKEVCRRVG
IEVEGKSVLELAQEVGEKALEDFRRLKGEGEATWLMTTINEGRKEKFRTH
NVVPFGIHASISELVNQAHMGMDNDPVNLVFSAIRVALADYTGEHIATDF
SDILFGTPQPVVSEANMGVLDPDQVNFVLHGHNPLLSEIIVQAAREMEGE
AKAAGAKGINLVGICCTGNEVLMRQGIPLVTSFASQELAICTGAIDAMCV
DVQCIMPSISAVAECYHTRIITTADNAKIPGAYHIDYQTATAIESAKTAI
RMAIEAFKERKESNRPVYIPQIKNRVVAGWSLEALTKLLATQNAQNPIRV
LNQAILDGELAGVALICGCNNLKGFQDNSHLTVMKELLKNNVFVVATGCS
AQAAGKLGLLDPANVETYCGDGLKGFLKRLGEGANIEIGLPPVFHMGSCV
DNSRAVDLLMAMANDLGVDTPKVPFVASAPEAMSGKAAAIGTWWVSLGVP
THVGTMPPVEGSDLIYSILTQIASDVYGGYFIFEMDPQVAARKILDALEY
RTWKLGVHKEVAERYETKLCQGY
3D structure
PDB1oao Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] Clusters in Closed and Open Alpha Subunits of Acetyl-Coa Synthase/Carbon Monoxide Dehydrogenase
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.7.4: anaerobic carbon-monoxide dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004601 peroxidase activity
GO:0016151 nickel cation binding
GO:0016491 oxidoreductase activity
GO:0043885 anaerobic carbon-monoxide dehydrogenase activity
GO:0046872 metal ion binding
GO:0050418 hydroxylamine reductase activity
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006091 generation of precursor metabolites and energy
GO:0015977 carbon fixation
GO:0042542 response to hydrogen peroxide
GO:0098869 cellular oxidant detoxification

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Molecular Function

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Biological Process
External links
PDB RCSB:1oao, PDBe:1oao, PDBj:1oao
PDBsum1oao
PubMed12627225
UniProtP27989|DCMB_MOOTH Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta

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