› 3tb9

X-ray diffraction
2.53Å resolution

Structure of Yeast Ribonucleotide Reductase 1 Q288A with AMPPNP and CDP

Released:
DOI: 10.2210/pdb3tb9/pdb
PDB entry 3tb9 coloured by chain, front view.
PDB entry 3tb9 coloured by chain, side view.
PDB entry 3tb9 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase.
Ahmad MF, Kaushal PS, Wan Q, Wijerathna SR, An X, Huang M, Dealwis CG
J Mol Biol 419 315-29 (2012)
PMID: 22465672

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-149283 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase large chain 1 Chain: A
Molecule details ›
Chain: A
Length: 888 amino acids
Theoretical weight: 99.62 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21524 (Residues: 1-888; Coverage: 100%)
Gene names: CRT7, RIR1, RNR1, SDS12, YER070W
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

3 bound ligands:
Ligand CDP 1 x CDP
Ligand ANP 1 x ANP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21212
Unit cell:
a: 107.886Å b: 116.959Å c: 64.329Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The structural basis for the allosteric regulation of ribonucleotide reductase.
Ahmad et al. (2013)
1 more

2 mentions without citation

Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase.
Ahmad et al. (2012)
1 more