PDBe 2r99

X-ray diffraction
1.61Å resolution

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

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Davis T, Newman EM, Mackenzie F, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (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)