PDBe 2gw2

X-ray diffraction
1.8Å resolution

Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G

Released:
Source organism: Homo sapiens
Entry authors: Bernstein G, Tempel W, Davis T, Newman EM, Finerty Jr PJ, Mackenzie F, Weigelt J, 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 G Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 21.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13427 (Residues: 1-179; Coverage: 24%)
Gene name: PPIG
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P212121
Unit cell:
a: 37.432Å b: 65.504Å c: 69.341Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.279
Expression system: Escherichia coli