1clh Summary



The structure was published by Clubb, R.T., Ferguson, S.B., Walsh, C.T., and Wagner, G., in 1994 in a paper entitled "Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin" (abstract).

The structure was determined using NMR spectroscopy and deposited in 1993.

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 P0AFL3 (PPIA_ECOLI)search. The sample contained 166 residues which is 100% of the natural sequence. Out of 166 residues 166 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 CYCLOPHILIN P0AFL3 (25-190) (PPIA_ECOLI)search Escherichia coli K-12search 100% 166 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0AFL3 (25 - 190) CYCLOPHILIN Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P0AFL3) 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 (P0AFL3) protein foldingsearch protein peptidyl-prolyl isomerizationsearch peptidyl-prolyl cis-trans isomerase activitysearch isomerase activitysearch periplasmic spacesearch outer membrane-bounded periplasmic spacesearch

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