› 2x7k

X-ray diffraction
1.15Å resolution

The crystal structure of PPIL1 in complex with cyclosporine A suggests a binding mode for SKIP

Released:
DOI: 10.2210/pdb2x7k/pdb
PDB entry 2x7k coloured by chain, front view.
PDB entry 2x7k coloured by chain, side view.
PDB entry 2x7k coloured by chain, top view.
Source organisms:
Primary publication:
The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein.
Stegmann CM, Lührmann R, Wahl MC
PLoS One 5 e10013 (2010)
PMID: 20368803

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163308 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase-like 1 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3C6 (Residues: 1-166; Coverage: 100%)
Gene names: CGI-124, CYPL1, PPIL1, UNQ2425/PRO4984
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
CYCLOSPORIN A Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand CD 2 x CD
Ligand NA 1 x NA
6 modified residues:
Ligand DAL 1 x DAL
Ligand MLE 4 x MLE
Ligand MVA 1 x MVA
Ligand BMT 1 x BMT
Ligand ABA 1 x ABA
Ligand SAR 1 x SAR

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21212
Unit cell:
a: 103.218Å b: 35.701Å c: 45.851Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.128 0.149
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems.
Sterpone et al. (2014)
1 more

7 mentions without citation

Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein-Protein Interactions.
Cardote et al. (2016)
6 more