Structure of PDB 7zcp Chain A Binding Site BS04
Receptor Information
>7zcp Chain A (length=341) Species:
566679
(Bradyrhizobium sp. ORS 375) [
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DDLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGT
TFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALG
GGALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMV
LPRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDT
EEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHL
IGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTH
NLIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGSTNE
Ligand information
Ligand ID
NO
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
ChEMBL
CHEMBL1234765
DrugBank
ZINC
PDB chain
7zcp Chain A Residue 410 [
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Receptor-Ligand Complex Structure
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PDB
7zcp
Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.
Resolution
1.29 Å
Binding residue
(original residue number in PDB)
D92 H94 H129
Binding residue
(residue number reindexed from 1)
D91 H93 H128
Annotation score
1
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
PDBsum
7zcp
PubMed
35862453
UniProt
H0SLX7
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