Structure of PDB 8rfp Chain A Binding Site BS03

Receptor Information
>8rfp Chain A (length=334) Species: 224911 (Bradyrhizobium diazoefficiens USDA 110) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLKLPRQKVELVAPPFVHAHEQATKQGPKIVEFKLTIEEKKVVIDEKGTT
FQAMTFNGSMPGPLMVVHEGDYVETTLVNPATNTMPHNIDFHSATGALGG
GALTLINPGEQVVLRWKATKTGVFVYHCAPGGPMIPWHVVSGMNGAVMVL
PRDGLNDGKGHALKYDKVYYVGEQDMYVPRDEKGNFKSYDSPGEAFTDTE
EMMKKLIPSHVVFNGKVGALTGKNALTANVGENVLIVHSQANRDSRPHLI
GGHGDYVWETGKFGNAPEVGLETWFIRGGSAGAAMYKFMQPGIYAYVTHN
LIEAADLCATAHFKVEGKWNDDLMTQVKAPAEIP
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain8rfp Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8rfp Spectroscopically validated pH-dependent MSOX movies provide detailed mechanism of copper nitrite reductases.
Resolution1.23 Å
Binding residue
(original residue number in PDB)		H94 H129
Binding residue
(residue number reindexed from 1)		H92 H127
Annotation score1
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity
Biological Process
GO:0019333 denitrification pathway
GO:0042128 nitrate assimilation
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8rfp, PDBe:8rfp, PDBj:8rfp
PDBsum8rfp
PubMed39002715
UniProtQ89EJ6

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