3uqi

X-ray diffraction
1.3Å resolution

Crystallographic structure of FKBP12 from Aedes aegypti

Released:
Source organism: Aedes aegypti
Entry authors: Sreekanth R, Saw KQ, Yoon HS

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidylprolyl isomerase Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 11.55 KDa
Source organism: Aedes aegypti
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1HR83 (Residues: 1-108; Coverage: 100%)
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 29.826Å b: 38.677Å c: 79.589Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.19
Expression system: Escherichia coli