› 1a33

X-ray diffraction
2.15Å resolution

PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI

Released:
DOI: 10.2210/pdb1a33/pdb
PDB entry 1a33 coloured by chain, front view.
PDB entry 1a33 coloured by chain, side view.
PDB entry 1a33 coloured by chain, top view.
Source organism: Brugia malayi
Primary publication:
Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi.
Mikol V, Ma D, Carlow CK
Protein Sci 7 1310-6 (1998)
PMID: 9655334

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
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P41212
Unit cell:
a: 57.9Å b: 57.9Å c: 140.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 0.211
Expression system: Escherichia coli

Quick links

Citations

2 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)
1 more

2 mentions without citation

Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis.
Ramanathan et al. (2011)
1 more