X-ray diffraction
2.8Å resolution

Structure of a peptide derived from Cdc9 bound to PCNA


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:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proliferating cell nuclear antigen Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 28.94 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P15873 (Residues: 1-258; Coverage: 100%)
Gene names: POL30, YBR0811, YBR088C
Sequence domains:
Structure domains: Proliferating Cell Nuclear Antigen
DNA ligase 1 Chain: B
Molecule details ›
Chain: B
Length: 22 amino acids
Theoretical weight: 2.46 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
  • Canonical: P04819 (Residues: 32-53; Coverage: 3%)
Gene names: CDC9, YDL164C

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: I23
Unit cell:
a: 139.28Å b: 139.28Å c: 139.28Å
α: 90° β: 90° γ: 90°
R R work R free
0.249 0.247 0.285
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided