PDBe 2awg

X-ray diffraction
1.6Å resolution

Structure of the PPIase domain of the Human FK506-binding protein 8

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Davis T, Newman EM, Finerty P, Mackenzie F, Weigelt J, Sundstrom M, Arrowsmith C, Edwards A, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP8 Chain: A
Molecule details ›
Chain: A
Length: 118 amino acids
Theoretical weight: 12.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14318 (Residues: 90-205; Coverage: 28%)
Gene names: FKBP38, FKBP8
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 FR-E
Spacegroup: P21
Unit cell:
a: 30.911Å b: 53.795Å c: 30.64Å
α: 90° β: 92.43° γ: 90°
R-values:
R R work R free
0.169 0.167 0.202
Expression system: Escherichia coli BL21(DE3)