PDBe 3lpy

X-ray diffraction
2Å resolution

Crystal structure of the RRM domain of CyP33

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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. (a.k.a. RRM, RBD, or RNP domain)
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:

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