› 4x3v

X-ray diffraction
3.7Å resolution

Crystal structure of human ribonucleotide reductase 1 bound to inhibitor

Released:
DOI: 10.2210/pdb4x3v/pdb
PDB entry 4x3v coloured by chain, front view.
PDB entry 4x3v coloured by chain, side view.
PDB entry 4x3v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of Non-nucleoside Human Ribonucleotide Reductase Modulators.
Ahmad MF, Huff SE, Pink J, Alam I, Zhang A, Perry K, Harris ME, Misko T, Porwal SK, Oleinick NL, Miyagi M, Viswanathan R, Dealwis CG
J Med Chem 58 9498-509 (2015)
PMID: 26488902

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:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase large subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 792 amino acids
Theoretical weight: 90.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23921 (Residues: 1-792; Coverage: 100%)
Gene names: RR1, RRM1
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

2 bound ligands:
Ligand TTP 2 x TTP
Ligand 3X4 1 x 3X4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 71.88Å b: 110.498Å c: 216.721Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.232 0.289
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Mechanisms and Factors That Drive Extensive Human Immunodeficiency Virus Type-1 Hypervariability: An Overview.
Yaseen et al. (2017)
2 more

1 mention without citation

Induction of cell cycle arrest and apoptosis by copper complex Cu(SBCM)2 towards oestrogen-receptor positive MCF-7 breast cancer cells.
Foo et al. (2019)