PDBe 1a7x

X-ray diffraction
2Å resolution

FKBP12-FK1012 COMPLEX

Released:
Source organism: Homo sapiens
Primary publication:
Chemical inducers of dimerization: the atomic structure of FKBP12-FK1012A-FKBP12.
Bioorg. Med. Chem. Lett. 8 1-6 (1998)
PMID: 9871618

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 107 amino acids
Theoretical weight: 11.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 133.59Å b: 40.51Å c: 93.13Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli