2pv3 Summary

pdbe.org/2pv3
spacer

Crystallographic Structure of SurA fragment lacking the second peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK

The structure was published by Xu, X., Wang, S., Hu, Y.X., and McKay, D.B., in 2007 in a paper entitled "The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.39 Å and deposited in 2007.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Chaperone surA and C-peptide.

The molecule most likely forms heterotrimers.

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 Chaperone surA P0ABZ6 (21-428) (SURA_ECOLI)search Escherichia coli K-12search 100% 299 94%
B Chaperone surA P0ABZ6 (21-428) (SURA_ECOLI)search Escherichia coli K-12search 100% 299 94%
C C-peptide Not available
Not available Not available 12 83%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0ABZ6 (21 - 428) Chaperone surA Escherichia coli

Chain Structural classification (SCOP) Sequence family (Pfam)
A, B (P0ABZ6) Porin chaperone SurA, peptide-binding domainsearch, FKBP immunophilin/proline isomerasesearch PF00639: PPIC-type PPIASE domainsearch, PF09312: SurA N-terminal domainsearch
C

Chain ID Molecular function (GO) Biological process (GO)
A, B (P0ABZ6) isomerase activitysearch protein foldingsearch protein transportsearch

Chain InterPro annotation
A, B Peptidyl-prolyl cis-trans isomerase, PpiC-typesearch SurA N-terminalsearch Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved sitesearch Trigger factor/SurA domainsearch
C