1bc2 Summary



The structure was published by Fabiane, S.M., Sohi, M.K., Wan, T., et al., Bateson, J.H., Mitchell, T., and Sutton, B.J., in 1998 in a paper entitled "Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1997.

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

This PDB entry contains multiple copies of the structure of METALLO-BETA-LACTAMASE II.

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 most likely forms homodimers.

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 METALLO-BETA-LACTAMASE II P04190 (31-257) (BLA2_BACCE)search Bacillus cereussearch 93% 227 95%
B METALLO-BETA-LACTAMASE II P04190 (31-257) (BLA2_BACCE)search Bacillus cereussearch 93% 227 95%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04190 (31 - 257) METALLO-BETA-LACTAMASE II Bacillus cereus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P04190) Zn metallo-beta-lactamasesearch Metallo-beta-lactamase, chain Asearch PF00753: Metallo-beta-lactamase superfamilysearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P04190) metal ion bindingsearch zinc ion bindingsearch beta-lactamase activitysearch hydrolase activitysearch antibiotic catabolic processsearch response to antibioticsearch

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