5mav

X-ray diffraction
2.58Å resolution

Crystal structure of human PCNA in complex with PARG (poly(ADP-ribose) glycohydrolase) peptide.

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-146057 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proliferating cell nuclear antigen Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 264 amino acids
Theoretical weight: 29.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12004 (Residues: 1-261; Coverage: 100%)
Gene name: PCNA
Sequence domains:
Structure domains: Proliferating Cell Nuclear Antigen
poly(ADP-ribose) glycohydrolase Chains: G, H, K, L, M, N
Molecule details ›
Chains: G, H, K, L, M, N
Length: 19 amino acids
Theoretical weight: 2.24 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q0MQR4 (Residues: 402-420; Coverage: 2%)
Gene name: PARG

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 77.597Å b: 153.604Å c: 85.512Å
α: 90° β: 96.9° γ: 90°
R-values:
R R work R free
0.241 0.239 0.291
Expression systems:
  • Escherichia coli
  • Not provided