6dwj

X-ray diffraction
2.5Å resolution

SAMHD1 Bound to Vidarabine-TP in the Catalytic Pocket

Released:

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
Macromolecule:
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)
UniProt:
  • Canonical: Q9Y3Z3 (Residues: 113-626; Coverage: 82%)
Gene names: MOP5, SAMHD1
Sequence domains: HD domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P21
Unit cell:
a: 86.862Å b: 146.724Å c: 99.594Å
α: 90° β: 114.45° γ: 90°
R-values:
R R work R free
0.177 0.175 0.208
Expression system: Escherichia coli BL21(DE3)