PDBe 1n1a

X-ray diffraction
2.4Å resolution

Crystal Structure of the N-terminal domain of human FKBP52

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the N-terminal domain of human FKBP52.
Acta Crystallogr. D Biol. Crystallogr. 59 16-22 (2003)
PMID: 12499534

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed Chains: A, B
Molecule details ›
Chains: A, B
Length: 140 amino acids
Theoretical weight: 15.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02790 (Residues: 1-140; Coverage: 31%)
Gene names: FKBP4, FKBP52
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 27.805Å b: 58.362Å c: 70.904Å
α: 90° β: 98.31° γ: 90°
R-values:
R R work R free
0.219 0.204 0.28
Expression system: Escherichia coli BL21(DE3)