1ci8 Summary



The structure was published by Wagner, U.G., Petersen, E.I., Schwab, H., and Kratky, C., in 2002 in a paper entitled "EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of PROTEIN (CARBOXYLESTERASE).

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 PROTEIN (CARBOXYLESTERASE) Q9KX40 (1-392) (ESTB_BURGA)search Burkholderia gladiolisearch 100% 392 96%
B PROTEIN (CARBOXYLESTERASE) Q9KX40 (1-392) (ESTB_BURGA)search Burkholderia gladiolisearch 100% 392 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9KX40 (1 - 392) PROTEIN (CARBOXYLESTERASE) Burkholderia gladioli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q9KX40) beta-Lactamase/D-ala carboxypeptidasesearch DD-peptidase/beta-lactamase superfamilysearch PF00144: Beta-lactamasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (Q9KX40) hydrolase activitysearch metabolic processsearch cytoplasmsearch

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