3zua Summary


A C39-like domain

The structure was published by Lecher, J., Schwarz, C.K.W., Stoldt, M., Smits, S.S.H., Willbold, D., and Schmitt, L., in 2012 in a paper entitled "An Rtx Transporter Tethers its Unfolded Substrate During Secretion Via a Unique N-Terminal Domain." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2011.

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

The PDB entry contains the structure of ALPHA-HEMOLYSIN TRANSLOCATION ATP-BINDING PROTEIN HLYB. This molecule has the UniProt identifier Q47258 (HLYB3_ECOLX)search. The sample contained 142 residues which is < 90% of the natural sequence. Out of 142 residues 142 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 ALPHA-HEMOLYSIN TRANSLOCATION ATP-BINDING PROTEIN HLYB Q47258 (2-137) (HLYB3_ECOLX)search Escherichia colisearch < 90% 142 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB

Chain Structural classification (CATH) Sequence family (Pfam)
A Cysteine proteinasessearch Peptidase C39 familysearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (Q47258) peptidase activitysearch ATP bindingsearch integral component of membranesearch proteolysissearch

Chain InterPro annotation
A Peptidase C39, bacteriocin processingsearch