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Yorodumi- PDB-1a2o: STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHOR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1a2o | ||||||
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Title | STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN | ||||||
Components | CHEB METHYLESTERASE | ||||||
Keywords | BACTERIAL CHEMOTAXIS / ADAPTATION / SERINE HYDROLASE | ||||||
Function / homology | Function and homology information protein-glutamate methylesterase / protein-glutamate methylesterase activity / protein-glutamine glutaminase activity / protein-glutamine glutaminase / phosphorelay response regulator activity / chemotaxis / cytoplasm Similarity search - Function | ||||||
Biological species | Salmonella typhimurium (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Djordjevic, S. / Goudreau, P.N. / Xu, Q. / Stock, A.M. / West, A.H. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1998 Title: Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Authors: Djordjevic, S. / Goudreau, P.N. / Xu, Q. / Stock, A.M. / West, A.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a2o.cif.gz | 147.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a2o.ent.gz | 116.8 KB | Display | PDB format |
PDBx/mmJSON format | 1a2o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a2o_validation.pdf.gz | 425.1 KB | Display | wwPDB validaton report |
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Full document | 1a2o_full_validation.pdf.gz | 468 KB | Display | |
Data in XML | 1a2o_validation.xml.gz | 36 KB | Display | |
Data in CIF | 1a2o_validation.cif.gz | 50.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a2/1a2o ftp://data.pdbj.org/pub/pdb/validation_reports/a2/1a2o | HTTPS FTP |
-Related structure data
Related structure data | 1chdS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 37598.852 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella typhimurium (bacteria) / Cellular location: CYTOPLASM / Plasmid: PME30 / Cell (production host): HB101 / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli (E. coli) References: UniProt: P04042, protein-glutamate methylesterase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.17 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jan 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. obs: 32281 / % possible obs: 96.9 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Biso Wilson estimate: 38.4 Å2 / Rsym value: 0.054 / Net I/σ(I): 7.5 |
Reflection shell | Resolution: 2.4→2.46 Å / Redundancy: 3.1 % / Mean I/σ(I) obs: 4.1 / Rsym value: 0.163 / % possible all: 98.5 |
Reflection | *PLUS Num. measured all: 97667 / Rmerge(I) obs: 0.054 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1CHD Resolution: 2.4→10 Å / Cross valid method: FREE R / σ(F): 0
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Displacement parameters | Biso mean: 23.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 32281 / Rfactor all: 0.222 / Rfactor Rfree: 0.288 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |