Function and Biology Details
Reaction catalysed:
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Ribonucleotide reductase large subunit, C-terminal
- Ribonucleotide reductase small subunit family
- Ribonucleotide reductase, class I, alpha subunit, C-terminal
- ATP-cone domain
- Ribonucleotide reductase small subunit, acitve site
- Ribonucleotide reductase small subunit
- Ferritin-like superfamily
- Ribonucleotide reductase-like
3 more domains
Structure analysis Details
Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177076 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonucleoside-diphosphate reductase
Molecule details ›
Chains: A, B, C, D
Length: 773 amino acids
Theoretical weight: 87.08 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 773 amino acids
Theoretical weight: 87.08 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
- Canonical:
Q5F8Z6 (Residues: 1-759; Coverage: 100%)
Sequence domains:
ribonucleoside-diphosphate reductase
Molecule details ›
Chains: E, F, G, H
Length: 391 amino acids
Theoretical weight: 45.11 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
Sequence domains: Ribonucleotide reductase, small chain
Length: 391 amino acids
Theoretical weight: 45.11 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
- Canonical: Q5F8Z5 (Residues: 8-384; Coverage: 98%)
Sequence domains: Ribonucleotide reductase, small chain
