|Entry||Database: PDB / ID: 1lhj|
|Title||ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS|
|Function / homology|
Function and homology information
Amyloid fiber formation / Antimicrobial peptides / Neutrophil degranulation / antimicrobial humoral response / azurophil granule lumen / specific granule lumen / retina homeostasis / tertiary granule lumen / lysozyme / killing of cells of other organism ...Amyloid fiber formation / Antimicrobial peptides / Neutrophil degranulation / antimicrobial humoral response / azurophil granule lumen / specific granule lumen / retina homeostasis / tertiary granule lumen / lysozyme / killing of cells of other organism / lysozyme activity / cytolysis / defense response to Gram-negative bacterium / inflammatory response / defense response to Gram-positive bacterium / defense response to bacterium / cellular protein metabolic process / neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding
Glycoside hydrolase, family 22, lysozyme / C-type lysozyme/alpha-lactalbumin family / Glycoside hydrolase, family 22, conserved site / Lysozyme-like domain superfamily / Lysozyme C / Glycoside hydrolase, family 22 / Glycosyl hydrolases family 22 (GH22) domain profile. / Glycosyl hydrolases family 22 (GH22) domain signature.
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / Resolution: 1.8 Å|
|Authors||Inaka, K. / Matsushima, M. / Herning, T. / Kuroki, R. / Yutani, K. / Kikuchi, M.|
Journal: Biochemistry / Year: 1992
Title: Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants.
Authors: Herning, T. / Yutani, K. / Inaka, K. / Kuroki, R. / Matsushima, M. / Kikuchi, M.
#1: Journal: J.Biol.Chem. / Year: 1991
Title: Crystal Structures of the Apo-and Holomutant Human Lysozymes with an Introduced Ca Binding Site
Authors: Inaka, K. / Kuroki, R. / Kikuchi, M. / Matsushima, M.
#2: Journal: Biochemistry / Year: 1991
Title: Effects of Proline Mutations on the Unfolding and Refolding of Human Lysozyme: The Slow Refolding Kinitics Phase Does not Result from Proline Cis-Trans Isomerization
Authors: Herning, T. / Yutani, K. / Taniyama, Y. / Kikuchi, M.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: HUMAN LYSOZYME
|#1: Protein/peptide|| |
Mass: 14680.631 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P61626, lysozyme
|#2: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION|
|Crystal||Density Matthews: 1.99 Å3/Da / Density % sol: 38.23 %|
*PLUSTemperature: 13 ℃ / pH: 5.8 / Method: unknown
|Components of the solutions|
Crystal-ID: 1 / Sol-ID: 1
|Radiation||Scattering type: x-ray|
|Radiation wavelength||Relative weight: 1|
*PLUSHighest resolution: 1.8 Å / Num. obs: 9358 / % possible obs: 82 % / Num. measured all: 39581 / Rmerge(I) obs: 0.034
|Software||Name: PROLSQ / Classification: refinement|
|Refinement||Resolution: 1.8→5 Å / |
|Refinement step||Cycle: LAST / Resolution: 1.8→5 Å|
|Refine LS restraints|
*PLUSName: PROLSQ / Classification: refinement
*PLUSHighest resolution: 1.8 Å / Num. reflection obs: 9358 / Rfactor obs: 0.152 / Lowest resolution: 5 Å
|Refine LS restraints|
|LS refinement shell|
*PLUSHighest resolution: 1.8 Å / Lowest resolution: 1.89 Å / Rfactor obs: 0.187
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