STRUCTURE OF HEN EGG-WHITE LYSOZYME
The structure was published by Weiss, M.S., Palm, G.J., and Hilgenfeld, R., in 2000 in a paper entitled "Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.65 Å and deposited in 1999.
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 P00698 (LYSC_CHICK). The sample contained 129 residues which is 100% of the natural sequence. Out of 129 residues 128 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):
This entry contains 1 unique UniProt protein: