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BioLiP

Structure of PDB 1h2a Chain L

Receptor sequence
>1h2aL (length=534) Species: 883 (Nitratidesulfovibrio vulgaris str. 'Miyazaki F') [Search protein sequence]
SSYSGPIVVDPVTRIEGHLRIEVEVENGKVKNAYSSSTLFRGLEIILKGR
DPRDAQHFTQRTCGVCTYTHALASTRCVDNAVGVHIPKNATYIRNLVLGA
QYLHDHIVHFYHLHALDFVDVTAALKADPAKAAKVASSISPRKTTAADLK
AVQDKLKTFVETGQLGPFTNAYFLGGHPAYYLDPETNLIATAHYLEALRL
QVKAARAMAVFGAKNPHTQFTVVGGVTCYDALTPQRIAEFEALWKETKAF
VDEVYIPDLLVVAAAYKDWTQYGGTDNFITFGEFPKDEYDLNSRFFKPGV
VFKRDFKNIKPFDKMQIEEHVRHSWYEGAEARHPWKGQTQPKYTDLHGDD
RYSWMKAPRYMGEPMETGPLAQVLIAYSQGHPKVKAVTDAVLAKLGVGPE
ALFSTLGRTAARGIETAVIAEYVGVMLQEYKDNIAKGDNVICAPWEMPKQ
AEGVGFVNAPRGGLSHWIRIEDGKIGNFQLVVPSTWTLGPRCDKNNVSPV
EASLIGTPVADAKRPVEILRTVHSFDPCIACGVH
3D structure
PDB1h2a Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis.
ChainL
Resolution1.8 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 MG L E62 L498 H552 E44 L480 H534
BS02 NFE L C81 C84 H88 R479 P501 S502 C546 C549 C63 C66 H70 R461 P483 S484 C528 C531
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:1h2a, PDBe:1h2a, PDBj:1h2a
PDBsum1h2a
PubMed9438867
UniProtP21852|PHNL_NITV9 Periplasmic [NiFe] hydrogenase large subunit (Gene Name=hydB)

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