1oba Summary



The structure was published by Hermoso, J.A., Monterroso, B., Albert, A., et al., Martinez-Ripoll, M., Garcia, J.L., and Menendez, M., in 2003 in a paper entitled "Structural Basis for Selective Recognition of Pneumococcal Cell Wall by Modular Endolysin from Phage Cp-1." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.45 Å and deposited in 2003.

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

The PDB entry contains the structure of LYSOZYME. This molecule has the UniProt identifier P15057 (LYS_BPCP1)search. The sample contained 339 residues which is 100% of the natural sequence. Out of 339 residues 334 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 LYSOZYME P15057 (1-339) (LYS_BPCP1)search Streptococcus phage Cp-1search 100% 339 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15057 (1 - 339) LYSOZYME Streptococcus phage Cp-1

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P15057) Cell wall binding repeatsearch, 1,4-beta-N-acetylmuraminidasesearch Glycosidasessearch, Cholin Bindingsearch, Multimodular pneumococcal cell wall endolysin, domain 3search PF01183: Glycosyl hydrolases family 25search, PF01473: Putative cell wall binding repeatsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P15057) defense response to bacteriumsearch peptidoglycan catabolic processsearch cell wall macromolecule catabolic processsearch cytolysissearch metabolic processsearch carbohydrate metabolic processsearch lysozyme activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch catalytic activitysearch

Chain InterPro annotation
A Glycoside hydrolase, family 25search Glycoside hydrolase, family 25, active sitesearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 25 subgroupsearch Cell wall/choline-binding repeatsearch