Structure of PDB 6qpt Chain B Binding Site BS02

Receptor Information

>6qpt Chain B (length=319) Species: 329 (Ralstonia pickettii)

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: 6qpt Chain B Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6qpt Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): H99 H134
• Binding residue (residue number reindexed from 1): H94 H129
• 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:6qpt, PDBe:6qpt, PDBj:6qpt
• PDBsum: 6qpt
• PubMed: 32051772
• UniProt: I6NAW4