Structure of PDB 5jsh Chain A

Receptor sequence
>5jshA (length=283) Species: 882 (Nitratidesulfovibrio vulgaris str. Hildenborough) [Search protein sequence]
GTLTGERPPVFWLQGQGCTGCSVTLLNSVHPSIADVLLKVISLEFHPTVM
AWEGEHAIEHMRKVAEKFKGKFFLVIEGSVPVEADGKYCIIGEANHHEIS
MVDALKEFGPNAAAVLAVGTCAAYGGIPAAEGSETGATAVSKFLGDNGIK
TPVVNIPGCPPHPDWIVGTVVLALDAIKKNGLEGGLAEVVKVLDSDGRPT
PFFGRNIHENCPYLDKYDEGVMSATFTDKVGCRYDLGCKGPMTMADCFER
KWNGGVNWCVQNAVCIGCVEPDFPDGKSPFYQA
3D structure
PDB5jsh The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis.
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C18 C21 C121 C159 H208 C211 C232 C238 C247 C259 C265 C268
Catalytic site (residue number reindexed from 1) C18 C21 C121 C159 H208 C211 C232 C238 C247 C259 C265 C268
Enzyme Commision number 1.12.2.1: cytochrome-c3 hydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008901 ferredoxin hydrogenase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0047806 cytochrome-c3 hydrogenase activity
GO:0051536 iron-sulfur cluster binding
GO:0051538 3 iron, 4 sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0009061 anaerobic respiration
Cellular Component
GO:0009375 ferredoxin hydrogenase complex
GO:0016020 membrane
GO:0042597 periplasmic space
GO:0044569 [Ni-Fe] hydrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5jsh, PDBe:5jsh, PDBj:5jsh
PDBsum5jsh
PubMed28319099
UniProtQ72AS4

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