[English] 日本語
![](img/lk-miru.gif)
- PDB-1ceh: STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF P... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ceh | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER | ||||||
![]() | PHOSPHOLIPASE A2 | ||||||
![]() | HYDROLASE (CARBOXYLIC ESTER) | ||||||
Function / homology | ![]() Acyl chain remodelling of PS / Acyl chain remodelling of PG / Synthesis of PA / Acyl chain remodelling of PC / Acyl chain remodelling of PE / Acyl chain remodelling of PI / positive regulation of podocyte apoptotic process / phosphatidylglycerol metabolic process / phosphatidylcholine metabolic process / calcium-dependent phospholipase A2 activity ...Acyl chain remodelling of PS / Acyl chain remodelling of PG / Synthesis of PA / Acyl chain remodelling of PC / Acyl chain remodelling of PE / Acyl chain remodelling of PI / positive regulation of podocyte apoptotic process / phosphatidylglycerol metabolic process / phosphatidylcholine metabolic process / calcium-dependent phospholipase A2 activity / phospholipase A2 / bile acid binding / arachidonic acid secretion / phospholipid metabolic process / lipid catabolic process / innate immune response in mucosa / phospholipid binding / fatty acid biosynthetic process / antimicrobial humoral immune response mediated by antimicrobial peptide / positive regulation of fibroblast proliferation / antibacterial humoral response / defense response to Gram-positive bacterium / signaling receptor binding / calcium ion binding / cell surface / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kumar, A. / Sekharudu, C. / Ramakrishnan, B. / Dupureur, C.M. / Zhu, H. / Tsai, M.-D. / Sundaralingam, M. | ||||||
![]() | ![]() Title: Structure and function of the catalytic site mutant Asp 99 Asn of phospholipase A2: absence of the conserved structural water. Authors: Kumar, A. / Sekharudu, C. / Ramakrishnan, B. / Dupureur, C.M. / Zhu, H. / Tsai, M.D. / Sundaralingam, M. #1: ![]() Title: Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence for the Interaction of Lysine-56 with Substrates Authors: Noel, J.P. / Bingman, C.A. / Deng, T. / Dupureur, C.M. / Hamilton, K.J. / Jiang, R.-T. / Kwak, J.-G. / Sekharudu, C. / Sundaralingam, M. / Tsai, M.-D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 38.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 26.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 414.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 417.8 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 10.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 13809.520 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
---|---|
#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.77 % | |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 7.6 / Method: unknown | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 10307 / % possible obs: 98.7 % |
Reflection | *PLUS Highest resolution: 1.9 Å / Observed criterion σ(F): 1 / Rmerge(I) obs: 0.06 |
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.9→6.5 Å / σ(F): 3
| ||||||||||||
Displacement parameters | Biso mean: 27.6 Å2 | ||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→6.5 Å
| ||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Rfactor obs: 0.185 / Rfactor Rwork: 0.185 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |