132l Summary

pdbe.org/132l
spacer

STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION

The structure was published by Rypniewski, W.R., Holden, H.M., and Rayment, I., in 1993 in a paper entitled "Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1993.

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

The PDB entry contains the structure of HEN EGG WHITE LYSOZYME. 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.

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

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