Structure of PDB 5jsk Chain A

Receptor sequence
>5jskA (length=283) Species: 882 (Nitratidesulfovibrio vulgaris str. Hildenborough) [Search protein sequence]
GTLTGERPPVFWLQGQGCTGCSVTLLNSVHPSIADVLLKVISLEFHPTVM
AWEGEHAIEHMRKVAEKFKGKFFLVIEGSVPVEADGKYCIIGEANHHEIS
MVDALKEFGPNAAAVLAVGTCAAYGGIPAAEGSETGATAVSKFLGDNGIK
TPVVNIPGCPPHPDWIVGTVVLALDAIKKNGLEGGLAEVVKVLDSDGRPT
PFFGRNIHENCPYLDKYDEGVMSATFTDKVGCRYDLGCKGPMTMADCFER
KWNGGVNWCVQNAVCIGCVEPDFPDGKSPFYQA
3D structure
PDB5jsk The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis.
ChainA
Resolution0.95 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
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SF4 A H208 C211 Y213 L214 C232 R233 Y234 C238 P241 V260 H208 C211 Y213 L214 C232 R233 Y234 C238 P241 V260
BS02 SF4 A I207 C247 W252 C259 C265 I266 C268 I207 C247 W252 C259 C265 I266 C268
BS03 SF4 A C18 G20 C21 G119 C121 C159 P160 C18 G20 C21 G119 C121 C159 P160
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:5jsk, PDBe:5jsk, PDBj:5jsk
PDBsum5jsk
PubMed28319099
UniProtQ72AS4

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