3mdf

X-ray diffraction
1.85Å resolution

Crystal structure of the RRM domain of Cyclophilin 33

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)
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: 85 amino acids
Theoretical weight: 9.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UNP9 (Residues: 1-83; Coverage: 28%)
Gene names: CYP33, PPIE
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 85.84Å b: 40.52Å c: 65.66Å
α: 90° β: 127.06° γ: 90°
R-values:
R R work R free
0.21 0.21 0.238
Expression system: Escherichia coli BL21(DE3)