Structure of PDB 1oqu Chain C

Receptor sequence

>1oquC (length=302) Species: 1697 (Corynebacterium ammoniagenes)

SNEYDEYIANHTDPVKAINWNVIPDEKDLEVWDRLTGNFWLPEKIPVSND
IQSWNKMTPQEQLATMRVFTGLTLLDTIQGTVGAISLLPDAETMHEEAVY
TNIAFMESVHAKSYSNIFMTLASTPQINEAFRWSEENENLQRKAKIIMSY
YNGDDPLKKKVASTLLESFLFYSGFYLPMYLSSRAKLTNTADIIRLIIRD
ESVHGYYIGYKYQQGVKKLSEAEQEEYKAYTFDLMYDLYENEIEYTEDIY
DDLGWTEDVKRFLRYNANKALNNLGYEGLFPTDETKVSPAILSSLSDDDW
DF

3D structure

• PDB: 1oqu A protein carboxylate coordinated oxo-centered tri-nuclear iron complex with possible implications for ferritin mineralization
• Chain: C
• Resolution: 2.0 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FE	C	D77 E108 H111 E202	D76 E107 H110 E201
BS02	FE	C	E108 E168 E202 H205	E107 E167 E201 H204
BS03	FE	C	E245 D324 D326 D328	E244 D297 D299 D301
BS04	FE	C	E248 D326 D328	E247 D299 D301
BS05	FE	C	E245 E248 D324	E244 E247 D297
BS06	OXY	C	E245 E248 D324 D326 D328	E244 E247 D297 D299 D301

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