Structure of PDB 6qpt Chain F Binding Site BS01

Receptor Information

>6qpt Chain F (length=320) Species: 329 (Ralstonia pickettii)

PGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISEG
VSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGPG
GGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILVE
PPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFNG
AEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGGT
NVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILKI
DGAENKLVYSGKELDSVYLG

Ligand information

• Ligand ID: NO2
• InChI: InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1
• InChIKey: IOVCWXUNBOPUCH-UHFFFAOYSA-M
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341: [O-]N=O
  OpenEye OEToolkits 1.5.0: N(=O)[O-]
• Formula: N O2
• Name: NITRITE ION
• DrugBank: DB12529
• PDB chain: 6qpt Chain E Residue 503

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): H240 I242 H289
• Binding residue (residue number reindexed from 1): H235 I237 H284
• Annotation score: 5

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