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Yorodumi- PDB-1asl: CRYSTAL STRUCTURES OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1asl | ||||||
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Title | CRYSTAL STRUCTURES OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE IN TWO CONFORMATIONS: COMPARISON OF AN UNLIGANDED OPEN AND TWO LIGANDED CLOSED FORMS | ||||||
Components | ASPARTATE AMINOTRANSFERASEAspartate transaminase | ||||||
Keywords | AMINOTRANSFERASE | ||||||
Function / homology | Function and homology information L-phenylalanine biosynthetic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine:2-oxoglutarate aminotransferase activity / aspartate catabolic 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: 2.6 Å | ||||||
Authors | Jaeger, J. / Jansonius, J.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms. Authors: Jager, J. / Moser, M. / Sauder, U. / Jansonius, J.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1asl.cif.gz | 167.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1asl.ent.gz | 133.2 KB | Display | PDB format |
PDBx/mmJSON format | 1asl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/1asl ftp://data.pdbj.org/pub/pdb/validation_reports/as/1asl | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO 138 AND PRO 195 OF BOTH CHAINS ARE CIS PROLINES. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99999, -0.00093, -0.00048), Vector: Details | THE ASYMMETRIC UNIT CONTAINS A DIMER OF ASPARTATE AMINOTRANSFERASE. | |
-Components
#1: Protein | Mass: 43619.215 Da / Num. of mol.: 2 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 #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THE RESIDUE NUMBERING USED IN THIS ENTRY CONFORMS TO THE AMINO ACID SEQUENCE OF THE CHICKEN ...THE RESIDUE NUMBERING USED IN THIS ENTRY CONFORMS TO THE AMINO ACID SEQUENCE OF THE CHICKEN CYTOSOLIC ISOENZYME. HENCE, THE RESIDUE NUMBERING STARTS WITH MET 5 AND RESIDUES 127, 128, 130, 131, 132, 153, 232 AND 406 OF BOTH CHAINS HAVE NOT BEEN INCLUDED. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.04 Å3/Da / Density % sol: 59.54 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: referred to 'Smith, D. L.', (1986) J. Mol. Biol., 191, 301-302 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.6 Å / Num. obs: 30388 / Num. measured all: 56280 / Rmerge(I) obs: 0.081 |
-Processing
Software |
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Refinement | Resolution: 2.6→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 10 Å / Num. reflection obs: 30112 / Rfactor obs: 0.183 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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