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Yorodumi- PDB-1j4j: Crystal Structure of Tabtoxin Resistance Protein (form II) comple... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1j4j | ||||||
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Title | Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A | ||||||
Components | TABTOXIN RESISTANCE PROTEIN | ||||||
Keywords | TRANSFERASE | ||||||
Function / homology | Function and homology information acyltransferase activity, transferring groups other than amino-acyl groups / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups Similarity search - Function | ||||||
Biological species | Pseudomonas syringae pv. tabaci (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.55 Å | ||||||
Authors | He, H. / Ding, Y. / Bartlam, M. / Zhang, R. / Duke, N. / Joachimiak, A. / Shao, Y. / Cao, Z. / Tang, H. / Liu, Y. ...He, H. / Ding, Y. / Bartlam, M. / Zhang, R. / Duke, N. / Joachimiak, A. / Shao, Y. / Cao, Z. / Tang, H. / Liu, Y. / Jiang, F. / Liu, J. / Zhao, N. / Rao, Z. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. Authors: He, H. / Ding, Y. / Bartlam, M. / Sun, F. / Le, Y. / Qin, X. / Tang, H. / Zhang, R. / Joachimiak, A. / Liu, J. / Zhao, N. / Rao, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1j4j.cif.gz | 83.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1j4j.ent.gz | 63.3 KB | Display | PDB format |
PDBx/mmJSON format | 1j4j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j4/1j4j ftp://data.pdbj.org/pub/pdb/validation_reports/j4/1j4j | HTTPS FTP |
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-Related 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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-Components
#1: Protein | Mass: 19445.549 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas syringae pv. tabaci (bacteria) Species: Pseudomonas amygdali / Plasmid: PQE-30 / Production host: Escherichia coli (E. coli) References: UniProt: P16966, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Chemical | #3: 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: 2.12 Å3/Da / Density % sol: 42.11 % |
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Crystal grow | Temperature: 291 K / Method: hanging drop/vapor diffusion / pH: 8 Details: PEG 4000, sodium acetate, Tris-HCL, pH 8.0, HANGING DROP/VAPOR DIFFUSION, temperature 291.0K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Aug 24, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→30 Å / Num. all: 15585 / Num. obs: 15493 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 3 % / Biso Wilson estimate: 13.4 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 18.7 |
Reflection shell | Resolution: 2.25→2.35 Å / Redundancy: 4.55 % / Rmerge(I) obs: 0.132 / Num. unique all: 1913 / % possible all: 98.7 |
-Processing
Software |
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Refinement | Resolution: 2.55→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber / Details: CNS
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Refinement step | Cycle: LAST / Resolution: 2.55→30 Å
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Refine LS restraints |
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