› 1c9h

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN

Released:
DOI: 10.2210/pdb1c9h/pdb
PDB entry 1c9h coloured by chain, front view.
PDB entry 1c9h coloured by chain, side view.
PDB entry 1c9h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of FKBP12.6 in complex with rapamycin.
Deivanayagam CC, Carson M, Thotakura A, Narayana SV, Chodavarapu RS
Acta Crystallogr D Biol Crystallogr 56 266-71 (2000)
PMID: 10713512

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-159281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1B Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68106 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP12.6, FKBP1B, FKBP1L, FKBP9, OTK4
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
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 45.696Å b: 49.288Å c: 51.694Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.249
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Regulation of ryanodine receptors by FK506 binding proteins.
Chelu et al. (2004)
4 more

13 mentions without citation

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