X-ray diffraction
1.05Å resolution

Crystal structure of the FK506-binding domain of human FKBP38


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidyl-prolyl cis-trans isomerase FKBP8 Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q14318 (Residues: 92-210; Coverage: 29%)
Gene names: FKBP38, FKBP8
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 29.057Å b: 60.288Å c: 30.84Å
α: 90° β: 97.59° γ: 90°
R R work R free
0.136 0.135 0.161
Expression system: Escherichia coli