Structure of PDB 8rfq Chain A Binding Site BS05

Receptor Information

>8rfq 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 ID

InChI

InChI=1S/HNO/c1-2/h1H

InChIKey

ODUCDPQEXGNKDN-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.385 OpenEye OEToolkits 2.0.7	[N]=O

Formula

N O

Name

NITRIC OXIDE;
Nitrogen monoxide

PDB chain

8rfq Chain A Residue 405 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	8rfq Spectroscopically validated pH-dependent MSOX movies provide detailed mechanism of copper nitrite reductases.
Resolution	1.32 Å
Binding residue (original residue number in PDB)	D92 H94 H129
Binding residue (residue number reindexed from 1)	D90 H92 H127
Annotation score	1

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:8rfq, PDBe:8rfq, PDBj:8rfq
PDBsum	8rfq
PubMed	39002715
UniProt	Q89EJ6

[Back to BioLiP]