1vai Summary

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Structure of e. coli cyclophilin B K163T mutant bound to n-acetyl-ala-ala-pro-ala-7-amino-4-methylcoumarin

The structure was published by Konno, M., Sano, Y., Okudaira, K., et al., Yamagishi-Ohmori, Y., Fushinobu, S., and Matsuzawa, H., in 2004 in a paper entitled "Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2004.

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

This PDB entry contains a complex of 2 biomacromolecules, namely cyclophilin B and (ACE)AAPA(MCM).

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 B P0AFL3 (25-190) (PPIA_ECOLI)search Escherichia coli K-12search 100% 166 100%
B cyclophilin B 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 B Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P0AFL3) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B (P0AFL3) periplasmic spacesearch outer membrane-bounded periplasmic spacesearch isomerase activitysearch peptidyl-prolyl cis-trans isomerase activitysearch protein foldingsearch protein peptidyl-prolyl isomerizationsearch

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