Structure of PDB 1frf Chain L

Receptor sequence
>1frfL (length=543) Species: 878 (Solidesulfovibrio fructosivorans) [Search protein sequence]
TPQSTFTGPIVVDPITRIEGHLRIMVEVENGKVKDAWSSSQLFRGLEIIL
KGRDPRDAQHFTQRACGVCTYVHALASSRCVDDAVKVSIPANARMMRNLV
MASQYLHDHLVHFYHLHALDWVDVTAALKADPNKAAKLAASIDTARTGNS
EKALKAVQDKLKAFVESGQLGIFTNAYFLGGHKAYYLPPEVNLIATAHYL
EALHMQVKAASAMAILGGKNPHTQFTVVGGCSNYQGLTKDPLANYLALSK
EVCQFVNECYIPDLLAVAGFYKDWGGIGGTSNYLAFGEFATDDSSPEKHL
ATSQFPSGVITGRDLGKVDNVDLGAIYEDVKYSWYAPGGDGKHPYDGVTD
PKYTKLDDKDHYSWMKAPRYKGKAMEVGPLARTFIAYAKGQPDFKKVVDM
VLGKLSVPATALHSTLGRTAARGIETAIVCANMEKWIKEMADSGAKDNTL
CAKWEMPEESKGVGLADAPRGSLSHWIRIKGKKIDNFQLVVPSTWNLGPR
GPQGDKSPVEEALIGTPIADPKRPVEILRTVHAFDPCIACGVH
3D structure
PDB1frf 3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis
ChainL
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 FE L C75 C546 C69 C540
BS02 MG L E53 L495 H549 E47 L489 H543
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:1frf, PDBe:1frf, PDBj:1frf
PDBsum1frf
PubMed9751716
UniProtP18188|PHNL_SOLFR Periplasmic [NiFe] hydrogenase large subunit (Gene Name=hydB)

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