1dyw Summary

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BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A DIVERGENT LOOP CYCLOPHILIN FROM CAENORHABDITIS ELEGANS

The structure was published by Dornan, J., Page, A.P., Taylor, P., et al., Winter, A.D., Husi, H., and Walkinshaw, M.D., in 1999 in a paper entitled "Biochemical and Structural Characterization of a Divergent Loop Cyclophilin from Caenorhabditis Elegans" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2000.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of CYCLOPHILIN 3. This molecule has the UniProt identifier P52011 (CYP3_CAEEL)search. The sample contained 173 residues which is 100% of the natural sequence. Out of 173 residues 172 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 3 P52011 (1-173) (CYP3_CAEEL)search Caenorhabditis eleganssearch 100% 173 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P52011 (1 - 173) CYCLOPHILIN 3 Caenorhabditis elegans

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P52011) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P52011) peptidyl-prolyl cis-trans isomerase activitysearch isomerase activitysearch protein bindingsearch cellsearch 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