PDBe 4rxq

X-ray diffraction
2.1Å resolution

The structure of GTP-dUTP-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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 Chains: A, B
Molecule details ›
Chains: A, B
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: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 150.8Å b: 108.915Å c: 92.217Å
α: 90° β: 122.73° γ: 90°
R-values:
R R work R free
0.198 0.197 0.229
Expression system: Escherichia coli