1o7e Summary

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CRYSTAL STRUCTURE OF THE CLASS A BETA-LACTAMSE L2 FROM STENOTROPHOMONAS MALTOPHILIA AT 1.51 ANGSTROM

A publication describing this structure is not available. The depositing authors are Pernot, L.search; Petrella, S.search; Sougakoff, W.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.51 Å and deposited in 2002.

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

This PDB entry contains multiple copies of the structure of L2 BETA LACTAMASE.

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 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 L2 BETA LACTAMASE Q9RBQ1 (28-303) (Q9RBQ1_STEMA)search Stenotrophomonas maltophiliasearch 98% 276 98%
B L2 BETA LACTAMASE Q9RBQ1 (28-303) (Q9RBQ1_STEMA)search Stenotrophomonas maltophiliasearch 98% 276 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9RBQ1 (28 - 303) L2 BETA LACTAMASE Stenotrophomonas maltophilia

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q9RBQ1) beta-Lactamase/D-ala carboxypeptidasesearch DD-peptidase/beta-lactamase superfamilysearch PF13354: Beta-lactamase enzyme familysearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q9RBQ1) response to antibioticsearch hydrolase activitysearch

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