Structure of PDB 1yrq Chain M

Receptor sequence
>1yrqM (length=545) Species: 878 (Solidesulfovibrio fructosivorans) [Search protein sequence]
KPTPQSTFTGPIVVDPITRIEGHLRIMVEVENGKVKDAWSSSQLFRGLEI
ILKGRDPRDAQHFTQRACGVCTYVHALASSRCVDDAVKVSIPANARMMRN
LVMASQYLHDHLVHFYHLHALDWVDVTAALKADPNKAAKLAASIAPARPG
NSAKALKAVQDKLKAFVESGQLGIFTNAYFLGGHKAYYLPPEVNLIATAH
YLEALHMQVKAASAMAILGGKNPHTQFTVVGGCSNYQGLTKDPLANYLAL
SKEVCQFVNECYIPDLLAVAGFYKDWGGIGGTSNYLAFGEFATDDSSPSK
HLATSQFPSGVITGRDLGKVDNVDLGAIYEDVKYSWYAPGGDGKHPYDGV
TDPKYTKLDDKDHYSWMKAPRYKGKAMEVGPLARTFIAYAKGQPDFKKVV
DMVLGKLSVPATALHSTLGRTAARGIETAIVCANMEKWIKEMADSGAKDN
TLCAKWEMPEESKGVGLADAPRGALSHWIRIKGKKIDNFQLVVPSTWNLG
PRGAQGDKSPVEEALIGTPIADPKRPVEILRTVHAFDPCIACGVH
3D structure
PDB1yrq Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.
ChainM
Resolution2.1 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 M R70 H228 R66 H224
BS02 MG M E53 L495 H549 E49 L491 H545
BS03 FCO M C75 V78 H79 P475 R476 L479 V497 P498 S499 C546 C71 V74 H75 P471 R472 L475 V493 P494 S495 C542
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:1yrq, PDBe:1yrq, PDBj:1yrq
PDBsum1yrq
PubMed15803334
UniProtP18188|PHNL_SOLFR Periplasmic [NiFe] hydrogenase large subunit (Gene Name=hydB)

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