4tvr

X-ray diffraction
2.29Å resolution

Tandem Tudor and PHD domains of UHRF2

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Dong A, Zhang Q, Ong M, Duan S, Li Y, Bountra C, Weigelt J, Edwards AM, Arrowsmith CH, Tong Y, Structural Genomics Consortium (SGC)

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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-572528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UHRF2 Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96PU4 (Residues: 109-395; Coverage: 35%)
Gene names: NIRF, RNF107, UHRF2
Sequence domains:
Structure domains: SH3 type barrels.

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 71.28Å b: 71.28Å c: 120.052Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.229 0.26
Expression system: Escherichia coli BL21(DE3)