› 3lpy

X-ray diffraction
2Å resolution

Crystal structure of the RRM domain of CyP33

Released:
DOI: 10.2210/pdb3lpy/pdb
PDB entry 3lpy coloured by chain, front view.
PDB entry 3lpy coloured by chain, side view.
PDB entry 3lpy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression.
Wang Z, Song J, Milne TA, Wang GG, Li H, Allis CD, Patel DJ
Cell 141 1183-94 (2010)
PMID: 20541251

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase E Chains: A, B
Molecule details ›
Chains: A, B
Length: 79 amino acids
Theoretical weight: 8.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNP9 (Residues: 5-82; Coverage: 26%)
Gene names: CYP33, PPIE
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand EPE 2 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P31
Unit cell:
a: 59.833Å b: 59.833Å c: 50.909Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.246
Expression system: Escherichia coli

Quick links

Citations

58 review citations

The bromodomain interaction module.
Filippakopoulos et al. (2012)
57 more

6 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
5 more