4dip

X-ray diffraction
1.82Å resolution

Crystal structure of human Peptidyl-prolyl cis-trans isomerase FKBP14

Released:
Source organism: Homo sapiens
Entry authors: Krojer T, Kiyani W, Goubin S, Muniz JRC, Filippakopoulos P, Arrowsmith CH, Edwards A, Bountra C, von Delft F, Oppermann U, Zschocke J, Yue WW, Structural Genomics Consortium (SGC)

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)
PDBe Complex ID:
PDB-CPX-192656 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP14 Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 125 amino acids
Theoretical weight: 14.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NWM8 (Residues: 19-138; Coverage: 62%)
Gene names: FKBP14, FKBP22, UNQ322/PRO381
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: DIAMOND BEAMLINE I03
Spacegroup: P1
Unit cell:
a: 63.12Å b: 64.06Å c: 80.81Å
α: 81.23° β: 75.21° γ: 73.38°
R-values:
R R work R free
0.205 0.203 0.231
Expression system: Escherichia coli