Structure of PDB 2frv Chain J

Receptor sequence
>2frvJ (length=530) Species: 879 (Megalodesulfovibrio gigas) [Search protein sequence]
NKIVVDPITRIEGHLRIEVEVEGGKIKNAWSMSTLFRGLEMILKGRDPRD
AQHFTQRACGVCTYVHALASVRAVDNCVGVKIPENATLMRNLTMGAQYMH
DHLVHFYHLHALDWVNVANALNADPAKAARLANDLSPKKTTTESLKAVQA
KVKALVESGQLGIFTNAYFLGGHPAYVLPAEVDLIATAHYLEALRVQVKA
ARAMAIFGAKNPHTQFTVVGGCTNYDSLRPERIAEFRKLYKEVREFIEQV
YITDLLAVAGFYKNWAGIGKTSNFLTCGEFPTDEYDLNSRYTPQGVIWGN
DLSKVDDFNPDLIEEHVKYSWYEGAGAHHPYKGVTKPKWTEFHGEDRYSW
MKAPRYKGEAFEVGPLASVLVAYAKKHEPTVKAVDLVLKTLGVGPEALFS
TLGRTAARGIQCLTAAQEVEVWLDKLEANVKAGKDDLYTDWQYPTESQGV
GFVNAPRGMLSHWIVQRGGKIENFQLVVPSTWNLGPRCAEGKLSAVEQAL
IGTPIADPKRPVEILRTVHSYDPCIACGVH
3D structure
PDB2frv Crystal Structure of the Nickel-Iron Hydrogenase from Desulfovibrio Gigas
ChainJ
Resolution2.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E18 C65 C68 H72 R463 S486 C530 C533
Catalytic site (residue number reindexed from 1) E12 C59 C62 H66 R457 S480 C524 C527
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 J R63 H219 R57 H213
BS02 MG J E46 L482 H536 E40 L476 H530
BS03 FCO J C68 A461 R463 V484 P485 S486 C533 C62 A455 R457 V478 P479 S480 C527
BS04 O J C68 R463 C530 C62 R457 C524
Gene Ontology
Molecular Function
GO:0008901 ferredoxin hydrogenase activity
GO:0016151 nickel cation binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0047806 cytochrome-c3 hydrogenase activity
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:2frv, PDBe:2frv, PDBj:2frv
PDBsum2frv
PubMed
UniProtP12944|PHNL_MEGGA Periplasmic [NiFe] hydrogenase large subunit (Gene Name=hydB)

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