2w3o

X-ray diffraction
1.85Å resolution

Crystal structure of the human PNKP FHA domain in complex with an XRCC1-derived phosphopeptide

Released:

Function and Biology Details

Reactions catalysed:
ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA
A 3'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-148467 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional polynucleotide phosphatase/kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 113 amino acids
Theoretical weight: 12.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96T60 (Residues: 1-110; Coverage: 21%)
Gene name: PNKP
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
DNA repair protein XRCC1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 1.02 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P18887 (Residues: 515-522; Coverage: 1%)
Gene name: XRCC1

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3
Unit cell:
a: 56.9Å b: 56.9Å c: 62.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.178 0.236
Expression systems:
  • Escherichia coli
  • Not provided