› 1lop

X-ray diffraction
1.8Å resolution

CYCLOPHILIN A COMPLEXED WITH SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE

Released:
DOI: 10.2210/pdb1lop/pdb
PDB entry 1lop coloured by chain, front view.
PDB entry 1lop coloured by chain, side view.
PDB entry 1lop coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer.
Konno M, Ito M, Hayano T, Takahashi N
J. Mol. Biol. 256 897-908 (1996)
PMID: 8601841

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-150085 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase B Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.2 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P23869 (Residues: 1-164; Coverage: 100%)
Gene names: JW0514, b0525, ppiB
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 477 Da
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 66.33Å b: 68.23Å c: 40.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Not provided

Quick links

Citations

2 review citations

Mitochondrial intermembrane junctional complexes and their role in cell death.
Crompton M. (2000)
1 more

6 mentions without citation

FOLD-RATE: prediction of protein folding rates from amino acid sequence.
Gromiha et al. (2006)
5 more