X-ray diffraction
1.7Å resolution

SAMHD1 Bound to Clofarabine-TP in the Catalytic Pocket and Allosteric Pocket


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 550 amino acids
Theoretical weight: 63.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9Y3Z3 (Residues: 113-626; Coverage: 82%)
Gene names: MOP5, SAMHD1
Sequence domains: HD domain

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 80.477Å b: 142.233Å c: 98.79Å
α: 90° β: 114.1° γ: 90°
R R work R free
0.178 0.176 0.202
Expression system: Escherichia coli BL21(DE3)