[English] 日本語
Yorodumi- PDB-4jey: E198A mutant of N-acetylornithine aminotransferase from Salmonell... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4jey | ||||||
---|---|---|---|---|---|---|---|
Title | E198A mutant of N-acetylornithine aminotransferase from Salmonella typhimurium | ||||||
Components | Acetylornithine/succinyldiaminopimelate aminotransferase | ||||||
Keywords | TRANSFERASE / PLP dependent fold type I sub class II family Aminotransferase | ||||||
Function / homology | Function and homology information succinyldiaminopimelate transaminase / succinyldiaminopimelate transaminase activity / acetylornithine transaminase / N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity / arginine biosynthetic process / lysine biosynthetic process via diaminopimelate / pyridoxal phosphate binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Salmonella typhimurium (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||
Authors | Bisht, S. / Bharath, S.R. / Murthy, M.R.N. | ||||||
Citation | Journal: To be Published Title: Conformational transitions, ligand specificity and catalysis in N-acetylornithine aminotransferase: Implications on drug designing and rational enzyme engineering in omega aminotransferases Authors: Bisht, S. / Bharath, S.R. / Murthy, M.R.N. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4jey.cif.gz | 177.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4jey.ent.gz | 138.9 KB | Display | PDB format |
PDBx/mmJSON format | 4jey.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/je/4jey ftp://data.pdbj.org/pub/pdb/validation_reports/je/4jey | HTTPS FTP |
---|
-Related structure data
Related structure data | 4jexC 4jezC 4jf0C 4jf1C 2pb0S S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 45680.922 Da / Num. of mol.: 2 / Mutation: E198A, A298T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella typhimurium (bacteria) / Strain: LT2 / Gene: argD, dapC, dtu, STM3468 / Plasmid: pRSET C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) Rosetta References: UniProt: P40732, acetylornithine transaminase, succinyldiaminopimelate transaminase |
---|
-Non-polymers , 5 types, 747 molecules
#2: Chemical | #3: Chemical | ChemComp-EDO / #4: Chemical | ChemComp-ACT / #5: Chemical | #6: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.35 % |
---|---|
Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 10.5 Details: 20% PEG 3350, 0.5M Ammonium acetate, 0.1M CAPS, pH 10.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9537 Å | |||||||||||||||||||||
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 18, 2012 / Details: Bent collimating mirror and toroid | |||||||||||||||||||||
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 | |||||||||||||||||||||
Reflection | Resolution: 1.55→111.86 Å / Num. obs: 94369 / % possible obs: 91.6 % / Redundancy: 6.4 % / Biso Wilson estimate: 12.7 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 16.9 | |||||||||||||||||||||
Reflection shell |
|
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2PB0 Resolution: 1.55→28 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.955 / SU B: 1.253 / SU ML: 0.046 / Cross valid method: THROUGHOUT / ESU R: 0.085 / ESU R Free: 0.082 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
| |||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.434 Å2
| |||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→28 Å
| |||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.55→1.59 Å / Total num. of bins used: 20
|