Structure of PDB 1oqu Chain A Binding Site BS01

Receptor Information

>1oqu Chain A (length=296) Species: 1697 (Corynebacterium ammoniagenes)

SNEYDEYIANHTDPVKAINWNVIPDEKDLEVWDRLTGNFWLPEKIPVSND
IQSWNKMTPQEQLATMRVFTGLTLLDTIQGTVGAISLLPDAETMHEEAVY
TNIAFMESVHAKSYSNIFMTLASTPQINEAFRWSEENENLQRKAKIIMSY
YNGDDPLKKKVASTLLESFLFYSGFYLPMYLSSRAKLTNTADIIRLIIRD
ESVHGYYIGYKYQQGVKKLSEAEQEEYKAYTFDLMYDLYENEIEYTEDIY
DDLGWTEDVKRFLRYNANKALNNLGYEGLFPTDETKVSPAILSSLS

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 1oqu Chain A Residue 1001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1oqu A protein carboxylate coordinated oxo-centered tri-nuclear iron complex with possible implications for ferritin mineralization
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D77 E108 H111 F172 E202
• Binding residue (residue number reindexed from 1): D76 E107 H110 F171 E201
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Y115 D201
• Catalytic site (residue number reindexed from 1): Y114 D200
• Enzyme Commision number: 1.17.4.1: ribonucleoside-diphosphate reductase.

Gene Ontology

Molecular Function

• GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009263 deoxyribonucleotide biosynthetic process

Cellular Component

• GO:0005971 ribonucleoside-diphosphate reductase complex

External links

• PDB: RCSB:1oqu, PDBe:1oqu, PDBj:1oqu
• PDBsum: 1oqu
• PubMed: 15178319
• UniProt: O69274