› 5d75

X-ray diffraction
1.83Å resolution

Crystal structure of Human FKBD25 in complex with FK506

Released:
DOI: 10.2210/pdb5d75/pdb
PDB entry 5d75 coloured by chain, front view.
PDB entry 5d75 coloured by chain, side view.
PDB entry 5d75 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.
Prakash A, Rajan S, Yoon HS
Protein Sci 25 905-10 (2016)
PMID: 26749369

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP3 Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 14.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q00688 (Residues: 109-224; Coverage: 52%)
Gene names: FKBP25, FKBP3
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

2 bound ligands:
Ligand FK5 1 x FK5
Ligand JEF 2 x JEF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P3221
Unit cell:
a: 74.784Å b: 74.784Å c: 44.618Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.187 0.233
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Comparative analysis of FKBP family protein: evaluation, structure, and function in mammals and Drosophila melanogaster.
Ghartey-Kwansah et al. (2018)
5 other articles

2 mentions without citation

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