Structure of PDB 7zcn Chain A Binding Site BS02

Receptor Information

>7zcn Chain A (length=341) Species: 566679 (Bradyrhizobium sp. ORS 375)

DDLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGT
TFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALG
GGALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMV
LPRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDT
EEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHL
IGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTH
NLIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGSTNE

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 7zcn Chain A Residue 405

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7zcn Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.
• Resolution: 1.19 Å
• Binding residue (original residue number in PDB): H89 C130 H140 M145
• Binding residue (residue number reindexed from 1): H88 C129 H139 M144
• 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

External links

• PDB: RCSB:7zcn, PDBe:7zcn, PDBj:7zcn
• PDBsum: 7zcn
• PubMed: 35862453
• UniProt: H0SLX7