[English] 日本語
![](img/lk-miru.gif)
- PDB-1c7p: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDU... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1c7p | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / EXTRA N-TERMINAL RESIDUES | ||||||
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 | ![]() ![]() | ||||||
![]() | Goda, S. / Takano, K. / Yamagata, Y. / Katakura, Y. / Yutani, K. | ||||||
![]() | ![]() Title: Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. Authors: Goda, S. / Takano, K. / Yamagata, Y. / Katakura, Y. / Yutani, K. #1: ![]() Title: Effect of Foreign N-terminal Residues on the Conformational Stability of Human Lysozyme Authors: Takano, K. / Tsuchimori, K. / Yamagata, Y. / Yutani, K. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 42.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 29.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 369.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 370.5 KB | Display | |
Data in XML | ![]() | 4.2 KB | Display | |
Data in CIF | ![]() | 6.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 15121.078 Da / Num. of mol.: 1 / Mutation: T15E, V16A, Q17E, G18A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||
---|---|---|---|
#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.67 Å3/Da / Density % sol: 66.49 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: cadmium chloride, sodium acetate, PEG 400, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 283K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 10 ℃Details: equal volume of protein and reservoir solution were used for the drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 283 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: WEISSENBERG / Detector: DIFFRACTOMETER / Date: Dec 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.4 Å / Num. all: 72761 / Num. obs: 9367 / % possible obs: 99.9 % / Rmerge(I) obs: 0.044 |
Reflection | *PLUS Num. measured all: 72761 |
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.4→5 Å /
| ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→5 Å
| ||||||||||||
Refine LS restraints |
|