Function and Biology Details
Reaction catalysed:
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-117856 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (3 distinct):
Multifunctional non-homologous end joining DNA repair protein LigD
Molecule details ›
Chains: A, B, C, D
Length: 303 amino acids
Theoretical weight: 32.83 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: LigD, primase-polymerase domain
Structure domains: Alpha-Beta Plaits
Length: 303 amino acids
Theoretical weight: 32.83 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P9WNV3 (Residues: 1-300; Coverage: 40%)
Sequence domains: LigD, primase-polymerase domain
Structure domains: Alpha-Beta Plaits
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007 HF
Spacegroup:
P21
Expression systems:
- Escherichia coli BL21(DE3)
- Not provided
