Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions

Summary for 1GAZ

Related2MEI 1GAY 1GB0 1GB2 1GB3 1GB5 1GB6 1GB7 1GB8 1GB9 1GBO 1GBW 1GBX 1GBY 1GBZ
DescriptorLYSOZYME, SODIUM ION (3 entities in total)
Functional Keywordssurface mutant, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14757.71
Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K. (deposition date: 2000-06-26, release date: 2000-07-27, Last modification date: 2018-03-14)
Primary citation
Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K.
Role of amino acid residues at turns in the conformational stability and folding of human lysozyme.
Biochemistry, 39:8655-8665, 2000
PubMed: 10913274 (PDB entries with the same primary citation)
DOI: 10.1021/bi9928694
MImport into Mendeley
Experimental method
NMR Information

Structure validation

ClashscoreRamachandran outliersSidechain outliers401.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution