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- PDB-1ild: OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ild | ||||||
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Title | OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6 | ||||||
![]() | OUTER MEMBRANE PHOSPHOLIPASE A | ||||||
![]() | HYDROLASE / MEMBRANE PROTEIN / ANTI-PARALLEL BETA BARREL / MEMBRANE PHOSPHOLIPASE / SERINE HYDROLASE / N156A | ||||||
Function / homology | ![]() phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / 1-acyl-2-lysophosphatidylserine acylhydrolase activity / phospholipase A1 activity / phospholipase activity / phosphatidylglycerol metabolic process / lysophospholipase activity / phospholipase A2 activity / phospholipase A2 / lipid catabolic process ...phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / 1-acyl-2-lysophosphatidylserine acylhydrolase activity / phospholipase A1 activity / phospholipase activity / phosphatidylglycerol metabolic process / lysophospholipase activity / phospholipase A2 activity / phospholipase A2 / lipid catabolic process / cell outer membrane / calcium ion binding / protein homodimerization activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Snijder, H.J. / Van Eerde, J.H. / Kingma, R.L. / Kalk, K.H. / Dekker, N. / Egmond, M.R. / Dijkstra, B.W. | ||||||
![]() | ![]() Title: Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad. Authors: Snijder, H.J. / Van Eerde, J.H. / Kingma, R.L. / Kalk, K.H. / Dekker, N. / Egmond, M.R. / Dijkstra, B.W. #1: ![]() Title: Structural Evidence for Dimerization-Regulated Activation of an Integral Membrane Phospholipase Authors: Snijder, H.J. / Ubarretxena-Belandia, I. / Blaauw, M. / Kalk, K.H. / Verheij, H.M. / Egmond, M.R. / Dekker, N. / Dijkstra, B.W. #2: ![]() Title: Crystallization and Preliminary X-Ray Analysis of Outer Membrane Phospholipase A from Escherichia Coli Authors: Blaauw, M. / Dekker, N. / Verheij, H.M. / Kalk, K.H. / Dijkstra, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 68.9 KB | Display | ![]() |
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PDB format | ![]() | 50.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 14 KB | Display | |
Data in CIF | ![]() | 17.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ilzC ![]() 1im0C ![]() 1qd5S S: Starting model for refinement C: citing same article ( |
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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
#1: Protein | Mass: 31493.852 Da / Num. of mol.: 1 / Mutation: N156A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Sugar | ChemComp-BOG / #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.13 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: MPD, calcium chloride, Bis-Tris buffer, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.6 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAC Science DIP-2000 / Detector: IMAGE PLATE / Date: Jan 15, 1999 / Details: mirrors |
Radiation | Monochromator: YALE MIRRORS + NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. obs: 9276 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Redundancy: 10 % / Rmerge(I) obs: 0.064 / Rsym value: 0.064 / Net I/σ(I): 25.4 |
Reflection shell | Resolution: 2.8→2.85 Å / Rmerge(I) obs: 0.343 / Mean I/σ(I) obs: 4.9 / Num. unique all: 453 / Rsym value: 0.343 / % possible all: 99.6 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 98747 |
Reflection shell | *PLUS % possible obs: 99.6 % / Num. unique obs: 453 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1QD5 MUTATED ACTIVE SITE RESIDUES to ALA AND GAVE ALL ATOMS A RANDOM SHIFT Resolution: 2.8→20 Å / Isotropic thermal model: anisotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber / Details: Bulk solvent correction.
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Displacement parameters |
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 20 Å / σ(F): 0 / Rfactor obs: 0.211 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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