5yco

X-ray diffraction
2.2Å resolution

Complex structure of PCNA with UHRF2

Released:
Source organism: Homo sapiens
Primary publication:
Structure insights into the molecular mechanism of the interaction between UHRF2 and PCNA.
Biochem Biophys Res Commun 494 575-580 (2017)
PMID: 28951215

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-146062 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proliferating cell nuclear antigen Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 269 amino acids
Theoretical weight: 29.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P12004 (Residues: 1-261; Coverage: 100%)
Gene name: PCNA
Sequence domains:
Structure domains: Proliferating Cell Nuclear Antigen
E3 ubiquitin-protein ligase UHRF2 Chains: E, F
Molecule details ›
Chains: E, F
Length: 17 amino acids
Theoretical weight: 2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96PU4 (Residues: 784-800; Coverage: 2%)
Gene names: NIRF, RNF107, UHRF2

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: R3
Unit cell:
a: 202.514Å b: 202.514Å c: 123.937Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.204 0.22
Expression systems:
  • Escherichia coli K-12
  • Not provided