3fwl Summary


Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli

The structure was published by Sung, M.T., Lai, Y.T., Huang, C.Y., et al., Cheng, W.C., Wong, C.H., and Ma, C., in 2009 in a paper entitled "Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.086 Å and deposited in 2009.

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

The PDB entry contains the structure of Penicillin-binding protein 1B. This molecule has the UniProt identifier P02919 (PBPB_ECOLI)search. The sample contained 751 residues which is < 90% of the natural sequence. Out of 751 residues 707 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

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 Penicillin-binding protein 1B P02919 (58-804) (PBPB_ECOLI)search Escherichia coli K-12search < 90% 751 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02919 (58 - 804) Penicillin-binding protein 1B Escherichia coli

Chain Structural classification (CATH) Sequence family (Pfam)
A Single alpha-helices involved in coiled-coils or other helix-helix interfacessearch, DD-peptidase/beta-lactamase superfamilysearch, Penicillin-binding protein 1b domainsearch, Penicillin binding protein transpeptidase domainsearch Penicillin binding protein transpeptidase domainsearch, Transglycosylasesearch, Transmembrane domain of transglycosylase PBP1 at N-terminalsearch, Bifunctional transglycosylase second domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P02919) response to antibioticsearch peptidoglycan biosynthetic processsearch peptidoglycan glycosyltransferase activitysearch peptidase activitysearch penicillin bindingsearch peptidoglycan-based cell wallsearch

Chain InterPro annotation
A Glycosyl transferase, family 51search Penicillin-binding protein, transpeptidasesearch Penicillin-binding protein 1Bsearch Beta-lactamase/transpeptidase-likesearch Lysozyme-like domainsearch Bifunctional transglycosylase second domainsearch