› 6dw3

X-ray diffraction
2.2Å resolution

SAMHD1 Bound to Cytarabine-TP in the Catalytic Pocket

Released:
DOI: 10.2210/pdb6dw3/pdb
PDB entry 6dw3 coloured by chain, front view.
PDB entry 6dw3 coloured by chain, side view.
PDB entry 6dw3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1.
Knecht KM, Buzovetsky O, Schneider C, Thomas D, Srikanth V, Kaderali L, Tofoleanu F, Reiss K, Ferreirós N, Geisslinger G, Batista VS, Ji X, Cinatl J, Keppler OT, Xiong Y
Proc Natl Acad Sci U S A 115 E10022-E10031 (2018)
PMID: 30305425

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: 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

4 bound ligands:
Ligand HF4 4 x HF4
Ligand DTP 4 x DTP
Ligand MG 8 x MG
Ligand GTP 4 x GTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 87.34Å b: 147.325Å c: 98.537Å
α: 90° β: 114.64° γ: 90°
R-values:
R R work R free
0.192 0.19 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

New strategies to treat AML: novel insights into AML survival pathways and combination therapies.
Nair et al. (2021)
6 more

1 mention without citation

The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1.
Knecht et al. (2018)