2hqj Summary


Cyclophilin from Leishmania major

A publication describing this structure is not available. The depositing authors are Arakaki, T.L.search; Merritt, E.A.search; Structural Genomics of Pathogenic Protozoa Consortium (SGPP)search

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2006.

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

The PDB entry contains the structure of Cyclophilin. This molecule has the UniProt identifier Q4QBH1 (Q4QBH1_LEIMA)search. The sample contained 183 residues which is < 90% of the natural sequence. Out of 183 residues 179 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

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 Cyclophilin Q4QBH1 (22-199) (Q4QBH1_LEIMA)search Leishmania majorsearch < 90% 183 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q4QBH1 (22 - 199) Cyclophilin Leishmania major

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

Chain ID Molecular function (GO) Biological process (GO)
A (Q4QBH1) peptidyl-prolyl cis-trans isomerase activitysearch protein foldingsearch protein peptidyl-prolyl isomerizationsearch

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