› 7etu

X-ray diffraction
1.39Å resolution

The FK1 domain of FKBP51 in complex with peptide-inhibitor hit SFPFT

Released:
DOI: 10.2210/pdb7etu/pdb
PDB entry 7etu coloured by chain, front view.
PDB entry 7etu coloured by chain, side view.
PDB entry 7etu coloured by chain, top view.
Source organisms:
Primary publication:
Discovery of pentapeptide-inhibitor hits targeting FKBP51 by combining computational modeling and X-ray crystallography.
Han JT, Zhu Y, Pan DB, Xue HX, Wang S, Peng Y, Liu H, He YX, Yao X
OpenAccess logo Comput Struct Biotechnol J 19 4079-4091 (2021)
PMID: 34401048

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-168254 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
peptide-inhibitor hit Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 598 Da
Source organism: synthetic construct
Expression system: Not provided
Peptidyl-prolyl cis-trans isomerase FKBP5 Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 14.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13451 (Residues: 16-140; Coverage: 27%)
Gene names: AIG6, FKBP5, FKBP51
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: SSRF BEAMLINE BL18U1
Spacegroup: P212121
Unit cell:
a: 42.326Å b: 54.425Å c: 56.319Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.196
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

1 mention without citation

Discovery of pentapeptide-inhibitor hits targeting FKBP51 by combining computational modeling and X-ray crystallography.
Han et al. (2021)