› 6yf2

X-ray diffraction
1.03Å resolution

Function and Biology Details

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

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: 109 amino acids
Theoretical weight: 11.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P62942 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

4 bound ligands:
Ligand OP5 1 x OP5
Ligand CD 1 x CD
Ligand CL 2 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P42212
Unit cell:
a: 57.482Å b: 57.482Å c: 54.469Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.141 0.149
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Current update on theranostic roles of cyclophilin A in kidney diseases.
Hadpech et al. (2022)
2 more