PDBe 1a33

X-ray diffraction
2.15Å resolution

PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI

Released:
Source organism: Brugia malayi

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (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