2vb1 Summary

pdbe.org/2vb1
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HEWL AT 0.65 ANGSTROM RESOLUTION

The structure was published by Wang, J., Dauter, M., Alkire, R., Joachimiak, A., and Dauter, Z., in 2007 in a paper entitled "Triclinic Lysozyme at 0.65 A Resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 0.65 Å and deposited in 2007.

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

The PDB entry contains the structure of LYSOZYME C. This molecule has the UniProt identifier P00698 (LYSC_CHICK)search. The sample contained 129 residues which is 100% of the natural sequence. Out of 129 residues 129 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 C P00698 (19-147) (LYSC_CHICK)search Gallus gallussearch 93% 129 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00698 (19 - 147) LYSOZYME C Gallus gallus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00698) C-type lysozymesearch Lysozymesearch PF00062: C-type lysozyme/alpha-lactalbumin familysearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00698) lysozyme activitysearch protein bindingsearch identical protein bindingsearch hydrolase activitysearch catalytic activitysearch hydrolase activity, acting on glycosyl bondssearch extracellular vesicular exosomesearch extracellular spacesearch extracellular regionsearch metabolic processsearch retina homeostasissearch defense response to bacteriumsearch cytolysissearch cell wall macromolecule catabolic processsearch

Chain InterPro annotation
A Glycoside hydrolase, family 22, lysozymesearch Glycoside hydrolase, family 22search Glycoside hydrolase, family 22, conserved sitesearch Lysozyme-like domainsearch Lysozyme Csearch