› 1e8k

X-ray diffraction
1.9Å resolution

Cyclophilin 3 Complexed With Dipeptide Ala-Pro

Released:
DOI: 10.2210/pdb1e8k/pdb
PDB entry 1e8k coloured by chain, front view.
PDB entry 1e8k coloured by chain, side view.
PDB entry 1e8k coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
The First Direct Determination of a Ligand Binding Constant in Protein Crystals.
Wu Sy SY, Dornan J, Kontopidis G, Taylor P, Walkinshaw MD
Angew Chem Int Ed Engl 40 582-586 (2001)
PMID: 11180378

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase 3 Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 18.58 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P52011 (Residues: 1-173; Coverage: 100%)
Gene names: Y75B12B.5, cyn-3, cyp-3
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

2 bound ligands:
Ligand ALA 1 x ALA
Ligand PRO 1 x PRO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P41212
Unit cell:
a: 61.035Å b: 61.035Å c: 122.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 not available 0.25
Expression system: Escherichia coli

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Citations

5 citation in other articles

Insights into cyclin groove recognition: complex crystal structures and inhibitor design through ligand exchange.
Kontopidis et al. (2003)
4 more