1btl Summary



The structure was published by Jelsch, C., Mourey, L., Masson, J.M., and Samama, J.P., in 1993 in a paper entitled "Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1993.

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

The PDB entry contains the structure of BETA-LACTAMASE TEM1. This molecule has the UniProt identifier P62593 (BLAT_ECOLX)search. The sample contained 263 residues which is 100% of the natural sequence. Out of 263 residues 263 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 BETA-LACTAMASE TEM1 P62593 (24-286) (BLAT_ECOLX)search Escherichia colisearch 93% 263 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62593 (24 - 286) BETA-LACTAMASE TEM1 Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P62593) beta-Lactamase/D-ala carboxypeptidasesearch DD-peptidase/beta-lactamase superfamilysearch PF13354: Beta-lactamase enzyme familysearch

Chain ID Molecular function (GO) Biological process (GO)
A (P62593) beta-lactamase activitysearch protein bindingsearch hydrolase activitysearch response to antibioticsearch beta-lactam antibiotic catabolic processsearch

Chain InterPro annotation
A Beta-lactamase, class-A/Dsearch Beta-lactamase/transpeptidase-likesearch Beta-lactamase, class-A active sitesearch