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- PDB-1psh: CRYSTAL STRUCTURE OF PHOSPHOLIPASE A2 FROM INDIAN COBRA REVEALS A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1psh | ||||||
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Title | CRYSTAL STRUCTURE OF PHOSPHOLIPASE A2 FROM INDIAN COBRA REVEALS A TRIMERIC ASSOCIATION | ||||||
![]() | PHOSPHOLIPASE A2 | ||||||
![]() | CARBOXYLIC ESTER HYDROLASE | ||||||
Function / homology | ![]() calcium-dependent phospholipase A2 activity / phospholipase A2 / arachidonate secretion / phospholipid metabolic process / lipid catabolic process / phospholipid binding / fatty acid biosynthetic process / positive regulation of fibroblast proliferation / signaling receptor binding / calcium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Fremont, D. / Xuong, N.-H. / Wilson, I. | ||||||
![]() | ![]() Title: Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric association. Authors: Fremont, D.H. / Anderson, D.H. / Wilson, I.A. / Dennis, E.A. / Xuong, N.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 82.3 KB | Display | ![]() |
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PDB format | ![]() | 63.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 13357.855 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.21 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8 / Method: microdialysis | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / % possible obs: 91.6 % / Observed criterion σ(I): 2 / Num. measured all: 226069 / Rmerge(I) obs: 0.047 |
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Processing
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Refinement | Resolution: 2.3→6 Å / σ(I): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 6 Å / Num. reflection all: 17542 / σ(I): 2 / Rfactor obs: 0.174 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.94 |