› 1a58

X-ray diffraction
1.95Å resolution

CYCLOPHILIN FROM BRUGIA MALAYI

Released:
DOI: 10.2210/pdb1a58/pdb
PDB entry 1a58 coloured by chain, front view.
PDB entry 1a58 coloured by chain, side view.
PDB entry 1a58 coloured by chain, top view.
Source organism: Brugia malayi
Primary publication:
The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi.
Taylor P, Page AP, Kontopidis G, Husi H, Walkinshaw MD
FEBS Lett 425 361-6 (1998)
PMID: 9559680

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase 1 Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 19.5 KDa
Source organism: Brugia malayi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27450 (Residues: 1-177; Coverage: 21%)
Gene name: CYP-1
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 58.215Å b: 58.215Å c: 141.944Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.233
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Peptidyl-prolyl cis-trans isomerases (immunophilins) and their roles in parasite biochemistry, host-parasite interaction and antiparasitic drug action.
Bell et al. (2006)
2 more

2 mentions without citation

Mapping the distribution of packing topologies within protein interiors shows predominant preference for specific packing motifs.
Basu et al. (2011)
1 more