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- PDB-1y6p: Crystal structure of disulfide engineered porcine pancratic phosp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1y6p | ||||||
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Title | Crystal structure of disulfide engineered porcine pancratic phospholipase a2 to group-x isozyme | ||||||
![]() | Phospholipase A2, major isoenzyme![]() | ||||||
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Function / homology | ![]() Acyl chain remodelling of PC / Acyl chain remodelling of PS / Acyl chain remodelling of PE / Acyl chain remodelling of PI / Acyl chain remodelling of PG / Synthesis of PA / positive regulation of podocyte apoptotic process / regulation of glucose import / phosphatidylglycerol metabolic process / phosphatidylcholine metabolic process ...Acyl chain remodelling of PC / Acyl chain remodelling of PS / Acyl chain remodelling of PE / Acyl chain remodelling of PI / Acyl chain remodelling of PG / Synthesis of PA / positive regulation of podocyte apoptotic process / regulation of glucose import / phosphatidylglycerol metabolic process / phosphatidylcholine metabolic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Yu, B.Z. / Pan, Y.H. / Jassen, M.J.W. / Bahnson, B.J. / Jain, M.K. | ||||||
![]() | ![]() Title: Kinetic and structural properties of disulfide engineered phospholipase a(2): insight into the role of disulfide bonding patterns. Authors: Yu, B.Z. / Pan, Y.H. / Janssen, M.J.W. / Bahnson, B.J. / Jain, M.K. #1: ![]() Title: Engineeering the disulphide bond patterns of secretory phospolipases A2 into porcine pancratic isozyme. The effects on folding, stability and enzymatic properties Authors: Janssen, M.J. / Verheij, H.M. / Slotboom, A.J. / Egmond, M.R. #2: ![]() Title: Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes Authors: Pan, Y.H. / Yu, B.Z. / Singer, A.G. / Ghomashchi, F. / Lambeau, G. / Jain, M.K. / Bahnson, B.J. | ||||||
History |
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Remark 999 | SEQUENCE C-terminal extension (residues 125-131) KGESDKC were added to model the disulfide bonding ...SEQUENCE C-terminal extension (residues 125-131) KGESDKC were added to model the disulfide bonding pattern of the group X enzyme. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 70 KB | Display | ![]() |
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PDB format | ![]() | 51.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1y6oC ![]() 1fxfS 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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1 | ![]()
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2 | ![]()
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3 |
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Unit cell |
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Details | The asymmetric unit contains two biological units: chain A and B. |
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Components
#1: Protein | ![]() Mass: 14712.515 Da / Num. of mol.: 2 / Mutation: M8L,M20L, N50C, c-terminal insertion KGESDKC Source method: isolated from a genetically manipulated source Details: M8L,M20L, N50C, c-terminal insertion KGESDKC (residues 125-131) Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | ![]() #4: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 43.8 % |
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 4000, Iso-Propanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 26, 2001 / Details: Mirrors |
Radiation | Monochromator: Yale Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.2→19.8 Å / Num. all: 11518 / Num. obs: 11340 / % possible obs: 98.6 % / Observed criterion σ(F): -3 / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Biso Wilson estimate: 20.8 Å2 / Rmerge(I) obs: 0.113 / Rsym value: 0.09 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.323 / Mean I/σ(I) obs: 3.7 / Num. unique all: 1092 / Rsym value: 0.3 / % possible all: 96.8 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB code 1FXF Resolution: 2.25→19.8 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 169796.85 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): -3 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.2004 Å2 / ksol: 0.325779 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.25→19.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.25→2.39 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 6
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Xplor file |
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