Structure of PDB 5aa5 Chain H

Receptor sequence
>5aa5H (length=345) Species: 381666 (Cupriavidus necator H16) [Search protein sequence]
AVPYGRKTQHTPALKEVHILWITAGLGCDGDSVSITAASQPSVEDVVLGA
IPGLPKVHLHNPVLAYENGDEFMAPFHKAARGEIDNFVLVLEGSIPNERI
NGEGYWAAMGTDPQTHQPITIPEWLDRLAPKALAVVGAGTCATYGGIHAM
EGNPTGCMGLADYLGWQWKSRAGLPIVNVPGCPVQPDNFMETLLYLLYQL
AGLAPMIPLDEALRPKWLFTRTVHDGCDRAGSYEQAIFATEYGNPNCIVK
LGCWGPVVQCNVPKRGWIAGVGGCPNVGGICIGCTMPGFPDKFMPFMDAP
PGAVLSSNLIKSYGPLIRSLRKLTKDTLNDEPKWRHNQPVLTTGY
3D structure
PDB5aa5 Structure of an Actinobacterial-Type [Nife]-Hydrogenase Reveals Insight Into O2-Tolerant H2 Oxidation.
ChainH
Resolution2.497 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C32 D35 C145 C186 H228 C231 C251 C257 V266 C278 C285 C288
Catalytic site (residue number reindexed from 1) C28 D31 C141 C182 H224 C227 C247 C253 V262 C274 C281 C284
Enzyme Commision number 1.12.99.6: hydrogenase (acceptor).
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 H H228 C231 R233 A234 C251 I252 V253 C257 G259 P279 H224 C227 R229 A230 C247 I248 V249 C253 G255 P275
BS02 SF4 H V227 C264 V266 C278 C285 I286 C288 T289 V223 C260 V262 C274 C281 I282 C284 T285
BS03 SF4 H C32 D35 G143 T144 C145 C186 P187 C28 D31 G139 T140 C141 C182 P183
Gene Ontology
Molecular Function
GO:0008901 ferredoxin hydrogenase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051538 3 iron, 4 sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0009061 anaerobic respiration
Cellular Component
GO:0009375 ferredoxin hydrogenase complex
GO:0016020 membrane
GO:0044569 [Ni-Fe] hydrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5aa5, PDBe:5aa5, PDBj:5aa5
PDBsum5aa5
PubMed26749450
UniProtQ7WXQ4

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