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). 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):
This entry contains 1 unique UniProt protein: