Function and Biology Details
Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- DNA-directed DNA-polymerase, family A, mitochondria
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Anticodon-binding
- Anticodon-binding domain superfamily
- POLG2, C-terminal
- Glycyl-tRNA synthetase/DNA polymerase subunit gamma-2
- DNA-directed DNA polymerase, family A, palm domain
- DNA-directed DNA polymerase, family A, conserved site
4 more domains
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Mitochondrial DNA polymerase gamma complex (preferred)
PDBe Complex ID:
PDB-CPX-156941 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA polymerase subunit gamma-1
Molecule details ›
Chains: A, D
Length: 1172 amino acids
Theoretical weight: 132.38 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: DNA mitochondrial polymerase exonuclease domain
Structure domains:
Length: 1172 amino acids
Theoretical weight: 132.38 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P54098 (Residues: 70-355, 356-1239; Coverage: 94%)
Sequence domains: DNA mitochondrial polymerase exonuclease domain
Structure domains:
DNA polymerase subunit gamma-2
Molecule details ›
Chains: B, C, E, F
Length: 427 amino acids
Theoretical weight: 48.76 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Anticodon binding domain
Structure domains:
Length: 427 amino acids
Theoretical weight: 48.76 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: Q9UHN1 (Residues: 59-485; Coverage: 88%)
Sequence domains: Anticodon binding domain
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P32
