› 6imn

X-ray diffraction
2.7Å resolution

The crystal structure of AsfvLIG:CT2 complex

Released:
DOI: 10.2210/pdb6imn/pdb
PDB entry 6imn coloured by chain, front view.
PDB entry 6imn coloured by chain, side view.
PDB entry 6imn coloured by chain, top view.
Source organisms:
Primary publication:
Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues.
Chen Y, Liu H, Yang C, Gao Y, Yu X, Chen X, Cui R, Zheng L, Li S, Li X, Ma J, Huang Z, Li J, Gan J
Nat Commun 10 387 (2019)
PMID: 30674878

Function and Biology Details

Reaction catalysed: 
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-120021 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 419 amino acids
Theoretical weight: 48.23 KDa
Source organism: African swine fever virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35970 (Residues: 1-419; Coverage: 100%)
Gene names: Ba71V-100, LIG, NP419L
Sequence domains: ATP dependent DNA ligase domain
DNA (5'-D(*CP*CP*AP*GP*TP*CP*CP*GP*AP*CP*CP*CP*GP*CP*AP*TP*CP*CP*CP*GP*GP*A)-3') Chains: C, F
Molecule details ›
Chains: C, F
Length: 22 nucleotides
Theoretical weight: 6.64 KDa
Source organism: synthetic construct
Expression system: Not provided
DNA (5'-D(*TP*CP*CP*GP*GP*GP*AP*TP*GP*CP*GP*TP*GP*TP*CP*GP*GP*AP*CP*TP*GP*G)-3') Chains: D, G
Molecule details ›
Chains: D, G
Length: 22 nucleotides
Theoretical weight: 6.84 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 58.235Å b: 113.989Å c: 243.068Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.247 0.268
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

3 review citations

Structures and Functional Diversities of ASFV Proteins.
Wang et al. (2021)
2 more