› 4msp

X-ray diffraction
1.9Å resolution

Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifs

Released:
DOI: 10.2210/pdb4msp/pdb
PDB entry 4msp coloured by chain, front view.
PDB entry 4msp coloured by chain, side view.
PDB entry 4msp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.
Boudko SP, Ishikawa Y, Nix J, Chapman MS, Bächinger HP
Protein Sci 23 67-75 (2014)
PMID: 24272907

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP14 Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 22.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NWM8 (Residues: 21-211; Coverage: 100%)
Gene names: FKBP14, FKBP22, UNQ322/PRO381
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 5 x CA
Ligand 1PE 2 x 1PE
Ligand PGO 8 x PGO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 36.43Å b: 101.2Å c: 58.97Å
α: 90° β: 100.01° γ: 90°
R-values:
R R work R free
0.16 0.158 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

The Ehlers-Danlos syndromes.
Malfait et al. (2020)
4 more

5 mentions without citation

FKBP Ligands-Where We Are and Where to Go?
Kolos et al. (2018)
4 more