PDBe 4rxo

X-ray diffraction
2.6Å resolution

The structure of GTP-bound SAMHD1

Released:
Source organism: Homo sapiens
Primary publication:
The mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP.
Acta Crystallogr. D Biol. Crystallogr. 71 516-24 (2015)
PMID: 25760601

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 539 amino acids
Theoretical weight: 62.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3Z3 (Residues: 109-626; Coverage: 83%)
Gene names: MOP5, SAMHD1
Sequence domains: HD domain
Structure domains: Hypothetical protein af1432

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P21
Unit cell:
a: 77.219Å b: 183.187Å c: 81.275Å
α: 90° β: 100.62° γ: 90°
R-values:
R R work R free
0.185 0.183 0.222
Expression system: Escherichia coli