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Yorodumi- PDB-1ase: THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE REC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ase | ||||||
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Title | THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH PLP-N-OXIDE | ||||||
Components | ASPARTATE AMINOTRANSFERASE | ||||||
Keywords | AMINOTRANSFERASE | ||||||
Function / homology | Function and homology information L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine-2-oxoglutarate transaminase activity / L-phenylalanine biosynthetic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / pyridoxal phosphate binding / protein homodimerization activity / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Schumacher, C. / Ringe, D. | ||||||
Citation | Journal: To be Published Title: The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with Plp-N-Oxide Authors: Schumacher, C. / Ringe, D. #1: Journal: Biochemistry / Year: 1991 Title: Activity and Structure of the Active Site Mutants R386Y and R386F of Escherichia Coli Aspartate Aminotransferase Authors: Danishefsky, A.T. / Onnufer, J.J. / Petsko, G.A. / Ringe, D. #2: Journal: Biochemistry / Year: 1989 Title: 2.8 Angstroms Resolution Crystal Structure of an Active Site Mutant of Aspartate Aminotransferase from Escherichia Coli Authors: Smith, D.L. / Almo, S.C. / Toney, M.D. / Ringe, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ase.cif.gz | 84 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ase.ent.gz | 63 KB | Display | PDB format |
PDBx/mmJSON format | 1ase.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/1ase ftp://data.pdbj.org/pub/pdb/validation_reports/as/1ase | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 140 / 2: CIS PROLINE - PRO 196 | ||||||||
Details | THE MOLECULE IS A DIMER. TO GENERATE THE OTHER CHAIN ONE MUST APPLY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, Y, 156.4-Z) TO THE COORDINATES IN THIS ENTRY. |
-Components
#1: Protein | Mass: 43619.215 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P00509, aspartate transaminase |
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#2: Chemical | ChemComp-NOP / |
#3: Chemical | ChemComp-MAE / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | HET GROUP NOP 258 IS BOUND TO LYS 258 FORMING A PROTONATED SCHIFF BASE LINKAGE (BETWEEN NZ LYS 258 ...HET GROUP NOP 258 IS BOUND TO LYS 258 FORMING A PROTONATED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.89 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.207 / Rfactor obs: 0.207 / Highest resolution: 2.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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