› 2r99

X-ray diffraction
1.61Å resolution

Crystal structure of cyclophilin ABH-like domain of human peptidylprolyl isomerase E isoform 1

Released:
DOI: 10.2210/pdb2r99/pdb
PDB entry 2r99 coloured by chain, front view.
PDB entry 2r99 coloured by chain, side view.
PDB entry 2r99 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.
Davis TL, Walker JR, Campagna-Slater V, Finerty PJ, Paramanathan R, Bernstein G, MacKenzie F, Tempel W, Ouyang H, Lee WH, Eisenmesser EZ, Dhe-Paganon S
PLoS Biol 8 e1000439 (2010)
PMID: 20676357

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 18.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UNP9 (Residues: 131-301; Coverage: 57%)
Gene names: CYP33, PPIE
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P42212
Unit cell:
a: 66.635Å b: 66.635Å c: 77.351Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.196
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

36 review citations

Host Factors in Coronavirus Replication.
de Wilde et al. (2018)
35 more

7 mentions without citation

Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.
Thapar R. (2015)
6 more