1sml Summary



The structure was published by Ullah, J.H., Walsh, T.R., Taylor, I.A., et al., Verma, C.S., Gamblin, S.J., and Spencer, J., in 1998 in a paper entitled "The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1998.

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

The PDB entry contains the structure of PROTEIN (PENICILLINASE). This molecule has the UniProt identifier P52700 (BLA1_STEMA)search. The sample contained 269 residues which is 100% of the natural sequence. Out of 269 residues 266 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 PROTEIN (PENICILLINASE) P52700 (22-290) (BLA1_STEMA)search Stenotrophomonas maltophiliasearch 100% 269 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P52700 (22 - 290) PROTEIN (PENICILLINASE) Stenotrophomonas maltophilia

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P52700) Zn metallo-beta-lactamasesearch Metallo-beta-lactamase, chain Asearch PF00753: Metallo-beta-lactamase superfamilysearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P52700) beta-lactamase activitysearch hydrolase activitysearch metal ion bindingsearch zinc ion bindingsearch periplasmic spacesearch response to antibioticsearch antibiotic catabolic processsearch

Chain InterPro annotation
A Beta-lactamase, class-B, conserved sitesearch Beta-lactamase-likesearch