PDBe 1q1c

X-ray diffraction
1.9Å resolution

Crystal structure of N(1-260) of human FKBP52

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02790 (Residues: 2-260; Coverage: 56%)
Gene names: FKBP4, FKBP52
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P21
Unit cell:
a: 48.829Å b: 42.218Å c: 79.065Å
α: 90° β: 102.25° γ: 90°
R-values:
R R work R free
0.211 0.208 0.247
Expression system: Escherichia coli