› 5a9j

X-ray diffraction
3.55Å resolution

Crystal structure of the Helicase domain of human DNA polymerase theta, apo-form

Released:
DOI: 10.2210/pdb5a9j/pdb
PDB entry 5a9j coloured by chain, front view.
PDB entry 5a9j coloured by chain, side view.
PDB entry 5a9j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.
Newman JA, Cooper CDO, Aitkenhead H, Gileadi O
OpenAccess logo Structure 23 2319-2330 (2015)
PMID: 26636256

Function and Biology Details

Reactions catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA polymerase theta Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 896 amino acids
Theoretical weight: 100.02 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O75417 (Residues: 1-894; Coverage: 35%)
Gene names: POLH, POLQ
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 128.017Å b: 130.531Å c: 160.91Å
α: 90° β: 100.77° γ: 90°
R-values:
R R work R free
0.227 0.225 0.265
Expression system: Spodoptera frugiperda

Quick links

Citations

20 review citations

DNA polymerase θ (POLQ), double-strand break repair, and cancer.
Wood et al. (2016)
19 more

8 mentions without citation

DNA Polymerase θ: A Unique Multifunctional End-Joining Machine.
Black et al. (2016)
7 more