› 1pbk

X-ray diffraction
2.5Å resolution

HOMOLOGOUS DOMAIN OF HUMAN FKBP25

Released:
DOI: 10.2210/pdb1pbk/pdb
PDB entry 1pbk coloured by chain, front view.
PDB entry 1pbk coloured by chain, side view.
PDB entry 1pbk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the human 25 kDa FK506 binding protein complexed with rapamycin.
Liang J, Hung DT, Schreiber SL, Clardy J
J. Am. Chem. Soc. 118 1231-1232 (1996)

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 domain:

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: 116 amino acids
Theoretical weight: 12.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

1 bound ligand:
Ligand RAP 1 x RAP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 86Å b: 86Å c: 55.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.243
Expression system: Escherichia coli

Quick links

Citations

7 mentions without citation

Structural coupling between FKBP12 and buried water.
Szep et al. (2009)
6 more