› 1vbs

X-ray diffraction
2Å resolution

STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE

Released:
DOI: 10.2210/pdb1vbs/pdb
PDB entry 1vbs coloured by chain, front view.
PDB entry 1vbs coloured by chain, side view.
PDB entry 1vbs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases.
Schiene C, Reimer U, Schutkowski M, Fischer G
FEBS Lett 432 202-6 (1998)
PMID: 9720925

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158787 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62937 (Residues: 2-165; Coverage: 99%)
Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
TETRAPEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 525 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand DAL 1 x DAL

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3221
Unit cell:
a: 67.1Å b: 67.1Å c: 95.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.247
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

The involvement of mammalian and plant FK506-binding proteins (FKBPs) in development.
Breiman et al. (2002)
2 more