› 4qfz

X-ray diffraction
2.3Å resolution

Crystal structure of the tetrameric dGTP/dTTP-bound SAMHD1 (RN206) mutant catalytic core

Released:
DOI: 10.2210/pdb4qfz/pdb
PDB entry 4qfz coloured by chain, front view.
PDB entry 4qfz coloured by chain, side view.
PDB entry 4qfz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.
Koharudin LM, Wu Y, DeLucia M, Mehrens J, Gronenborn AM, Ahn J
J Biol Chem 289 32617-27 (2014)
PMID: 25288794

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
Structure domains: Hypothetical protein af1432

Ligands and Environments

3 bound ligands:
Ligand DGT 4 x DGT
Ligand TTP 8 x TTP
Ligand MG 9 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 87.831Å b: 146.738Å c: 98.941Å
α: 90° β: 114.29° γ: 90°
R-values:
R R work R free
0.21 0.209 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Deoxyribonucleotide metabolism, mutagenesis and cancer.
Mathews CK. (2015)
10 more

1 mention without citation

Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.
Koharudin et al. (2014)