1LHL

ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

Summary for 1LHL

DescriptorHUMAN LYSOZYME (2 entities in total)
Functional Keywordshydrolase(o-glycosyl)
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14746.73
Authors
Inaka, K.,Matsushima, M.,Herning, T.,Kuroki, R.,Yutani, K.,Kikuchi, M. (deposition date: 1992-03-27, release date: 1994-01-31, Last modification date: 2017-11-29)
Primary citation
Herning, T.,Yutani, K.,Inaka, K.,Kuroki, R.,Matsushima, M.,Kikuchi, M.
Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants.
Biochemistry, 31:7077-7085, 1992
PubMed: 1643041 (PDB entries with the same primary citation)
DOI: 10.1021/bi00146a008
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
?

Structure validation

ClashscoreRamachandran outliersSidechain outliers300MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1lhl
no rotation
Molmil generated image of 1lhl
rotated about x axis by 90°
Molmil generated image of 1lhl
rotated about y axis by 90°