Structure of PDB 7zcp Chain A Binding Site BS04

Receptor Information
>7zcp Chain A (length=341) Species: 566679 (Bradyrhizobium sp. ORS 375) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DDLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGT
TFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALG
GGALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMV
LPRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDT
EEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHL
IGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTH
NLIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGSTNE
Ligand information
Ligand IDNO
InChIInChI=1S/HNO/c1-2/h1H
InChIKeyODUCDPQEXGNKDN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385
OpenEye OEToolkits 2.0.7
[N]=O
FormulaN O
NameNITRIC OXIDE;
Nitrogen monoxide
ChEMBLCHEMBL1234765
DrugBank
ZINC
PDB chain7zcp Chain A Residue 410 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7zcp Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.
Resolution1.29 Å
Binding residue
(original residue number in PDB)
D92 H94 H129
Binding residue
(residue number reindexed from 1)
D91 H93 H128
Annotation score1
Enzymatic activity
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
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:7zcp, PDBe:7zcp, PDBj:7zcp
PDBsum7zcp
PubMed35862453
UniProtH0SLX7

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