› 1h0p

X-ray diffraction
1.75Å resolution

Cyclophilin_5 from C. elegans

Released:
DOI: 10.2210/pdb1h0p/pdb
PDB entry 1h0p coloured by chain, front view.
PDB entry 1h0p coloured by chain, side view.
PDB entry 1h0p coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans.
Picken NC, Eschenlauer S, Taylor P, Page AP, Walkinshaw MD
J Mol Biol 322 15-25 (2002)
PMID: 12215411

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase 5 Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 19.89 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P52013 (Residues: 23-204; Coverage: 100%)
Gene names: F31C3.1, cyn-5, cyp-5
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

1 bound ligand:
Ligand DTT 1 x DTT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P61
Unit cell:
a: 94.115Å b: 94.115Å c: 41.239Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 not available 0.25
Expression system: Escherichia coli BL21(DE3)

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