1a33 Summary



The structure was published by Mikol, V., Ma, D., and Carlow, C.K., in 1998 in a paper entitled "Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.15 Å and deposited in 1998.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PEPTIDYLPROLYL ISOMERASE. This molecule has the UniProt identifier Q27450 (CYP1_BRUMA)search. The sample contained 177 residues which is < 90% of the natural sequence. Out of 177 residues 173 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PEPTIDYLPROLYL ISOMERASE Q27450 (1-177) (CYP1_BRUMA)search Brugia malayisearch < 90% 177 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q27450 (1 - 177) PEPTIDYLPROLYL ISOMERASE Brugia malayi

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Cyclophilin (peptidylprolyl isomerase)search Cyclophilin-likesearch Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q27450) peptidyl-prolyl cis-trans isomerase activitysearch protein peptidyl-prolyl isomerizationsearch protein foldingsearch

Chain InterPro annotation
A Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainsearch Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved sitesearch Cyclophilin-type peptidyl-prolyl cis-trans isomerasesearch Cyclophilin-like domainsearch