Structure of PDB 3h3x Chain S

Receptor sequence
>3h3xS (length=544) Species: 878 (Solidesulfovibrio fructosivorans) [Search protein sequence]
PTPQSTFTGPIVVDPITRIEGHLRIMVEVENGKVKDAWSSSQLFRGLEII
LKGRDPRDAQHFTQRACGMCTYVHALASSRCVDDAVKVSIPANARMMRNL
VMASQYLHDHLVHFYHLHALDWVDVTAALKADPNKAAKLAASIAPARPGN
SAKALKAVQDKLKAFVESGQLGIFTNAYFLGGHKAYYLPPEVDLIATAHY
LEALHMQVKAASAMAILGGKNPHTQFTVVGGCSNYQGLTKDPLANYLALS
KEVCQFVNECYIPDLLAVAGFYKDWGGIGGTSNYLAFGEFATDDSSPEKH
LATSQFPSGVITGRDLGKVDNVDLGAIYEDVKYSWYAPGGDGKHPYDGVT
DPKYTKLDDKDHYSWMKAPRYKGKAMEVGPLARTFIAYAKGQPDFKKVVD
MVLGKLSVPATALHSTLGRTAARGIETAIVCANMEKWIKEMADSGAKDNT
LCAKWEMPEESKGVGLADAPRGALSHWIRIKGKKIDNFQLVVPSTWNLGP
RGAQGDKSPVEEALIGTPIADPKRPVEILRTVHAFDPCIACGVH
3D structure
PDB3h3x Introduction of methionines in the gas channel makes [NiFe] hydrogenase aero-tolerant
ChainS
Resolution2.7 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 FCO S C75 V78 H79 A474 P475 R476 V497 P498 S499 C546 C70 V73 H74 A469 P470 R471 V492 P493 S494 C541
BS02 MG S E53 L495 H549 E48 L490 H544
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:3h3x, PDBe:3h3x, PDBj:3h3x
PDBsum3h3x
PubMed19580279
UniProtP18188|PHNL_SOLFR Periplasmic [NiFe] hydrogenase large subunit (Gene Name=hydB)

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