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Yorodumi- PDB-1aic: STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1aic | ||||||
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Title | STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL-5'-PHOSPHATE BINDING LYSINE RESIDUE | ||||||
Components | ASPARTATE AMINOTRANSFERASEAspartate transaminase | ||||||
Keywords | TRANSFERASE(AMINOTRANSFERASE) | ||||||
Function / homology | Function and homology information L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine:2-oxoglutarate aminotransferase 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: 2.4 Å | ||||||
Authors | Jaeger, J. / Jansonius, J.N. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue. Authors: Malashkevich, V.N. / Jager, J. / Ziak, M. / Sauder, U. / Gehring, H. / Christen, P. / 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 | 1aic.cif.gz | 162.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1aic.ent.gz | 128.1 KB | Display | PDB format |
PDBx/mmJSON format | 1aic.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ai/1aic ftp://data.pdbj.org/pub/pdb/validation_reports/ai/1aic | 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: CIS PROLINE - PRO A 138 / 2: CIS PROLINE - PRO A 195 / 3: CIS PROLINE - PRO B 138 / 4: CIS PROLINE - PRO B 195 5: GLU B 376 - PHE B 377 OMEGA = 148.23 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
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: 43628.180 Da / Num. of mol.: 2 / Mutation: K246H 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: Chemical | 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: 3.12 Å3/Da / Density % sol: 60.63 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||
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: 2.4 Å / Lowest resolution: 10 Å / Num. all: 39276 / Num. obs: 72346 / % possible obs: 93.1 % / Rmerge(I) obs: 0.047 |
-Processing
Software |
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Refinement | Resolution: 2.4→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.191 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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