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- PDB-2bax: Atomic Resolution Structure of the Double Mutant (K53,56M) of Bov... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bax | ||||||
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Title | Atomic Resolution Structure of the Double Mutant (K53,56M) of Bovine Pancreatic Phospholipase A2 | ||||||
![]() | Phospholipase A2 | ||||||
![]() | HYDROLASE / Phospholipase A2 / alpha helix / beta sheet | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Sekar, K. / Yogavel, M. / Velmurugan, D. / Dauter, Z. / Dauter, M. / Tsai, M.D. | ||||||
![]() | ![]() Title: Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2. Authors: Sekar, K. / Rajakannan, V. / Gayathri, D. / Velmurugan, D. / Poi, M.J. / Dauter, M. / Dauter, Z. / Tsai, M.D. #1: ![]() Title: Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 Authors: Sekar, K. / Rajakannan, V. / Gayathri, D. / Velmurugan, D. / Poi, M.J. / Dauter, M. / Dauter, Z. / Tsai, M.D. #2: ![]() Title: Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2. Authors: Sekar, K. / Mala, S.V. / Yogavel, M. / Velmurugan, D. / Poi, M.J. / Vishwanath, B.S. / Gowda, T.V. / Jeyaprakash, A.A. / Tsai, M.D. #3: ![]() Title: Observation of additional calcium ion in the crystal structure of the triple mutant K56,120,121M of bovine pancreatic phospholipase A2. Authors: Rajakannan, V. / Yogavel, M. / Poi, M.J. / Jeyaprakash, A.A. / Jeyakanthan, J. / Velmurugan, D. / Tsai, M.D. / Sekar, K. #4: ![]() Title: High-resolution refinement of orthorhombic bovine pancreatic phospholipase A2. Authors: Sekar, K. / Sundaralingam, M. #5: ![]() Title: Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99. Authors: Sekar, K. / Yu, B.Z. / Rogers, J. / Lutton, J. / Liu, X. / Chen, X. / Tsai, M.D. / Jain, M.K. / Sundaralingam, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.7 KB | Display | ![]() |
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PDB format | ![]() | 71.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 468.2 KB | Display | ![]() |
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Full document | ![]() | 479.2 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 18.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1vl9C ![]() 1c74S C: citing same article ( S: Starting model for refinement |
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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 on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 13814.536 Da / Num. of mol.: 1 / Mutation: K53M, K56M Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 216 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/MRD.gif)
![](data/chem/img/MPD.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/MRD.gif)
![](data/chem/img/MPD.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CA / | ||||
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#3: Chemical | ChemComp-CL / | ||||
#4: Chemical | ChemComp-MRD / ( #5: Chemical | ChemComp-MPD / ( | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.11 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 7.2 Details: The double mutant protein was dissolved in 50 mM Tris buffer (7.2) containing 5mM of CaCl2, to a final protein Concentration of 17-20 mg/ml. The crystallization droplet contained 5 micro ...Details: The double mutant protein was dissolved in 50 mM Tris buffer (7.2) containing 5mM of CaCl2, to a final protein Concentration of 17-20 mg/ml. The crystallization droplet contained 5 micro litre of protein and 2 micro litre of 60% MPD and the reservior contianined 1000 micro litre of 70% MPD, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→20 Å / Num. obs: 50297 / % possible obs: 98.2 % / Observed criterion σ(F): 4 / Rmerge(I) obs: 0.044 |
Reflection shell | Resolution: 1.1→1.14 Å / Rmerge(I) obs: 0.216 / Num. unique all: 50297 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1C74 Resolution: 1.1→20 Å / Cross valid method: THROUGHOUT / σ(F): 4 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.1→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.1→1.14 Å
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