Structure of PDB 6qpu Chain D Binding Site BS01

Receptor Information

>6qpu Chain D (length=319) Species: 658080 (Ralstonia sp. 5_2_56FAA)

PGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISEG
VSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGPG
GGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILVE
PPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFNG
AEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGGT
NVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILKI
DGAENKLVYSGKELDSVYL

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: 6qpu Chain D Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6qpu Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
• Resolution: 2.25 Å
• Binding residue (original residue number in PDB): H94 C135 H143
• Binding residue (residue number reindexed from 1): H89 C130 H138
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H94 D97 H99 H134 C135 H143 M148 H240 Q262 T263 H289
• Catalytic site (residue number reindexed from 1): H89 D92 H94 H129 C130 H138 M143 H235 Q257 T258 H284
• Enzyme Commision number: 1.7.2.1: nitrite reductase (NO-forming).

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0050421 nitrite reductase (NO-forming) activity

External links

• PDB: RCSB:6qpu, PDBe:6qpu, PDBj:6qpu
• PDBsum: 6qpu
• PubMed: 32051772
• UniProt: U3G913