› 7ltt

X-ray diffraction
1.9Å resolution

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-195223 (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: 535 amino acids
Theoretical weight: 61.85 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

2 bound ligands:
Ligand DGT 8 x DGT
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 80.926Å b: 140.105Å c: 97.193Å
α: 90° β: 114.18° γ: 90°
R-values:
R R work R free
0.179 0.178 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Targeting the DNA damage response and repair in cancer through nucleotide metabolism.
Helleday et al. (2022)
1 more

1 mention without citation

Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins.
Bowen et al. (2021)