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- PDB-1gay: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SUR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gay | ||||||
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Title | CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS | ||||||
![]() | MUTANT LYSOZYME | ||||||
![]() | HYDROLASE / surface mutant | ||||||
Function / homology | ![]() antimicrobial humoral response / Antimicrobial peptides / metabolic process / specific granule lumen / azurophil granule lumen / tertiary granule lumen / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism ...antimicrobial humoral response / Antimicrobial peptides / metabolic process / specific granule lumen / azurophil granule lumen / tertiary granule lumen / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / inflammatory response / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Funahashi, J. / Takano, K. / Yamagata, Y. / Yutani, K. | ||||||
![]() | ![]() Title: Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Authors: Funahashi, J. / Takano, K. / Yamagata, Y. / Yutani, K. #1: ![]() Title: Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme Authors: Funahashi, J. / Takano, K. / Yamagata, Y. / Yutani, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 44.5 KB | Display | ![]() |
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PDB format | ![]() | 30.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.2 KB | Display | ![]() |
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Full document | ![]() | 362 KB | Display | |
Data in XML | ![]() | 3.9 KB | Display | |
Data in CIF | ![]() | 7.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gb0C ![]() 1gb2C ![]() 1gb3C ![]() 1gb5C ![]() 1gb6C ![]() 1gb7C ![]() 1gb8C ![]() 1gb9C ![]() 1gboC ![]() 1gbwC ![]() 1gbxC ![]() 1gbyC ![]() 1gbzC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 14678.613 Da / Num. of mol.: 1 / Mutation: V2G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.91 Å3/Da / Density % sol: 35.44 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: sodium phosphate, sodium chloride, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 10 ℃Details: protein solution was mixed in a 1:1 ratio with reservoir solution | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jan 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54184 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.8 Å / Num. all: 29322 / Num. obs: 10116 / % possible obs: 92.1 % / Rmerge(I) obs: 0.074 |
Reflection | *PLUS Num. measured all: 29322 |
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Processing
Software | Name: ![]() | ||||||||||||
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Refinement | Resolution: 1.8→8 Å /
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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