Structure of PDB 1yq9 Chain I

Receptor sequence
>1yq9I (length=530) Species: 879 (Megalodesulfovibrio gigas) [Search protein sequence]
NKIVVDPITRIEGHLRIEVEVEGGKIKNAWSMSTLFRGLEMILKGRDPRD
AQHFTQRACGVCTYVHALASVRAVDNCVGVKIPENATLMRNLTMGAQYMH
DHLVHFYHLHALDWVNVANALNADPAKAARLANDLSPRKTTTESLKAVQA
KVKALVESGQLGIFTNAYFLGGHPAYVLPAEVDLIATAHYLEALRVQVKA
ARAMAIFGAKNPHTQFTVVGGCTNYDSLRPERIAEFRKLYKEVREFIEQV
YITDLLAVAGFYKNWAGIGKTSNFLTCGEFPTDEYDLNSRYTPQGVIWGN
DLSKVDDFNPDLIEEHVKYSWYEGADAHHPYKGVTKPKWTEFHGEDRYSW
MKAPRYKGEAFEVGPLASVLVAYAKKHEPTVKAVDLVLKTLGVGPEALFS
TLGRTAARGIQCLTAAQEVEVWLDKLEANVKAGKDDLYTDWQYPTESQGV
GFVNAPRGMLSHWIVQRGGKIENFQLVVPSTWNLGPRCAEGKLSAVEQAL
IGTPIADPKRPVEILRTVHSYDPCIACGVH
3D structure
PDB1yq9 Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.
ChainI
Resolution2.35 Å
3D
structure
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Enzymatic activity
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 I R63 H219 R57 H213
BS02 MG I E46 L482 H536 E40 L476 H530
BS03 FCO I C68 H72 R463 V484 P485 S486 C533 C62 H66 R457 V478 P479 S480 C527
BS04 PER I 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:1yq9, PDBe:1yq9, PDBj:1yq9
PDBsum1yq9
PubMed15803334
UniProtP12944|PHNL_MEGGA Periplasmic [NiFe] hydrogenase large subunit (Gene Name=hydB)

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