› 5tus

X-ray diffraction
2.66Å resolution

Potent competitive inhibition of human ribonucleotide reductase by a novel non-nucleoside small molecule

Released:
DOI: 10.2210/pdb5tus/pdb
PDB entry 5tus coloured by chain, front view.
PDB entry 5tus coloured by chain, side view.
PDB entry 5tus coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Potent competitive inhibition of human ribonucleotide reductase by a nonnucleoside small molecule.
Ahmad MF, Alam I, Huff SE, Pink J, Flanagan SA, Shewach D, Misko TA, Oleinick NL, Harte WE, Viswanathan R, Harris ME, Dealwis CG
Proc Natl Acad Sci U S A 114 8241-8246 (2017)
PMID: 28716944

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-150118 (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:

Ligands and Environments

3 bound ligands:
Ligand TTP 2 x TTP
Ligand MG 2 x MG
Ligand 7LL 1 x 7LL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 69.516Å b: 114.282Å c: 220.361Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.25
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Analysing central metabolism in ultra-high resolution: At the crossroads of carbon and nitrogen.
Bayram et al. (2020)
1 more

5 mentions without citation

Inhibitors of the Cancer Target Ribonucleotide Reductase, Past and Present.
Huff et al. (2022)
4 more