Structure of PDB 3h3x Chain R

Receptor sequence
>3h3xR (length=545) Species: 878 (Solidesulfovibrio fructosivorans) [Search protein sequence]
KPTPQSTFTGPIVVDPITRIEGHLRIMVEVENGKVKDAWSSSQLFRGLEI
ILKGRDPRDAQHFTQRACGMCTYVHALASSRCVDDAVKVSIPANARMMRN
LVMASQYLHDHLVHFYHLHALDWVDVTAALKADPNKAAKLAASIAPARPG
NSAKALKAVQDKLKAFVESGQLGIFTNAYFLGGHKAYYLPPEVDLIATAH
YLEALHMQVKAASAMAILGGKNPHTQFTVVGGCSNYQGLTKDPLANYLAL
SKEVCQFVNECYIPDLLAVAGFYKDWGGIGGTSNYLAFGEFATDDSSPEK
HLATSQFPSGVITGRDLGKVDNVDLGAIYEDVKYSWYAPGGDGKHPYDGV
TDPKYTKLDDKDHYSWMKAPRYKGKAMEVGPLARTFIAYAKGQPDFKKVV
DMVLGKLSVPATALHSTLGRTAARGIETAIVCANMEKWIKEMADSGAKDN
TLCAKWEMPEESKGVGLADAPRGALSHWIRIKGKKIDNFQLVVPSTWNLG
PRGAQGDKSPVEEALIGTPIADPKRPVEILRTVHAFDPCIACGVH
3D structure
PDB3h3x Introduction of methionines in the gas channel makes [NiFe] hydrogenase aero-tolerant
ChainR
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 R C75 H79 A474 P475 R476 L479 V497 P498 S499 C546 C71 H75 A470 P471 R472 L475 V493 P494 S495 C542
BS02 MG R E53 L495 H549 E49 L491 H545
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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