› 4qfy

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb4qfy/pdb
PDB 4qfy coloured by chain and viewed from the front.
PDB 4qfy coloured by chain and viewed from the side.
PDB 4qfy coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural basis of allosteric activation of Sterile Alpha 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. (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)
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 8 x DGT
Ligand DCP 4 x DCP
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 87.966Å b: 147.021Å c: 98.873Å
α: 90° β: 114.31° γ: 90°
R-values:
R R work R free
0.227 0.226 0.269
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Dendritic Cells, the Double Agent in the War Against HIV-1.
Martín-Moreno et al. (2019)
3 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)