5mgx

X-ray diffraction
2.18Å resolution

The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-136256 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent molecular chaperone HSP82 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 8 amino acids
Theoretical weight: 967 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P02829 (Residues: 702-709; Coverage: 1%)
Gene names: HSP82, HSP90, YPL240C
Peptidyl-prolyl cis-trans isomerase FKBP8 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 290 amino acids
Theoretical weight: 31.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14318 (Residues: 91-380; Coverage: 70%)
Gene names: FKBP38, FKBP8
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 74.29Å b: 105.64Å c: 100.19Å
α: 90° β: 93.1° γ: 90°
R-values:
R R work R free
0.249 0.246 0.308
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)