› 1fkh

X-ray diffraction
1.95Å resolution

DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12

Released:
DOI: 10.2210/pdb1fkh/pdb
PDB entry 1fkh coloured by chain, front view.
PDB entry 1fkh coloured by chain, side view.
PDB entry 1fkh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS AND THE X-RAY CRYSTAL-STRUCTURES OF THEIR COMPLEXES WITH FKBP12.
Holt DA, Luengo JI, Yamashita DS, Oh HJ, Konialian AL, Yen HK, Rozamus LW, Brandt M, Bossard MJ, Levy MA, Eggleston DS, Liang J, Schultz LW, Stout TJ, Clardy J
J. Am. Chem. Soc. 115 9925-9938 (1993)

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.84 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62942 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 31.45Å b: 43.38Å c: 77.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 not available
Expression system: Not provided

Quick links

Citations

9 mentions without citation

Accurate determination of protein:ligand standard binding free energies from molecular dynamics simulations.
Fu et al. (2022)
8 more