Structure of PDB 5aa5 Chain A Binding Site BS01

Receptor Information
>5aa5 Chain A (length=345) Species: 381666 (Cupriavidus necator H16) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVPYGRKTQHTPALKEVHILWITAGLGCDGDSVSITAASQPSVEDVVLGA
IPGLPKVHLHNPVLAYENGDEFMAPFHKAARGEIDNFVLVLEGSIPNERI
NGEGYWAAMGTDPQTHQPITIPEWLDRLAPKALAVVGAGTCATYGGIHAM
EGNPTGCMGLADYLGWQWKSRAGLPIVNVPGCPVQPDNFMETLLYLLYQL
AGLAPMIPLDEALRPKWLFTRTVHDGCDRAGSYEQAIFATEYGNPNCIVK
LGCWGPVVQCNVPKRGWIAGVGGCPNVGGICIGCTMPGFPDKFMPFMDAP
PGAVLSSNLIKSYGPLIRSLRKLTKDTLNDEPKWRHNQPVLTTGY
Ligand information
Ligand IDSF4
InChIInChI=1S/4Fe.4S
InChIKeyLJBDFODJNLIPKO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7[S]12[Fe]3[S]4[Fe]1[S]5[Fe]2[S]3[Fe]45
CACTVS 3.385S1[Fe]S[Fe]1.S2[Fe]S[Fe]2
FormulaFe4 S4
NameIRON/SULFUR CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain5aa5 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5aa5 Structure of an Actinobacterial-Type [Nife]-Hydrogenase Reveals Insight Into O2-Tolerant H2 Oxidation.
Resolution2.497 Å
Binding residue
(original residue number in PDB)		H228 C231 R233 A234 C251 I252 V253 C257 P279
Binding residue
(residue number reindexed from 1)		H224 C227 R229 A230 C247 I248 V249 C253 P275
Annotation score1
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).
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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