› 5hkg

X-ray diffraction
1.5Å resolution

Total chemical synthesis, refolding and crystallographic structure of a fully active immunophilin: calstabin 2 (FKBP12.6).

Released:
DOI: 10.2210/pdb5hkg/pdb
PDB entry 5hkg coloured by chain, front view.
PDB entry 5hkg coloured by chain, side view.
PDB entry 5hkg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2 (FKBP12.6).
Bacchi M, Jullian M, Sirigu S, Fould B, Huet T, Bruyand L, Antoine M, Vuillard L, Ronga L, Chavas LM, Nosjean O, Ferry G, Puget K, Boutin JA
Protein Sci 25 2225-2242 (2016)
PMID: 27670942

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1B Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.67 KDa
Source organism: Homo sapiens
Expression system: synthetic construct
UniProt:
  • Canonical: P68106 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP12.6, FKBP1B, FKBP1L, FKBP9, OTK4
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

3 bound ligands:
Ligand RAP 1 x RAP
Ligand CL 3 x CL
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 45.2Å b: 48.61Å c: 53.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.194
Expression system: synthetic construct

Quick links

Citations

1 review citation

General lack of structural characterization of chemically synthesized long peptides.
Boutin et al. (2019)
1 other article

3 mentions without citation

Macrocyclic FKBP51 Ligands Define a Transient Binding Mode with Enhanced Selectivity.
Voll et al. (2021)
2 more