1lop Summary



The structure was published by Konno, M., Ito, M., Hayano, T., and Takahashi, N., in 1996 in a paper entitled "The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1996.

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

This PDB entry contains a complex of 2 biomacromolecules, namely CYCLOPHILIN A and SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE.

The molecule most likely forms heterodimers.

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 A P23869 (1-164) (PPIB_ECOLI)search Escherichia coli K-12search 100% 164 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P23869 (1 - 164) CYCLOPHILIN A Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P23869) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P23869) protein foldingsearch protein peptidyl-prolyl isomerizationsearch peptidyl-prolyl cis-trans isomerase activitysearch protein bindingsearch isomerase activitysearch cytoplasmsearch cytosolsearch

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