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- PDB-1aaw: THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1aaw | ||||||
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Title | THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI | ||||||
![]() | ASPARTATE AMINOTRANSFERASE![]() | ||||||
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Function / homology | ![]() L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-phenylalanine biosynthetic process / ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Almo, S.C. / Smith, D.L. / Danishefsky, A.T. / Ringe, D. | ||||||
![]() | ![]() Title: The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Authors: Almo, S.C. / Smith, D.L. / Danishefsky, A.T. / Ringe, D. #1: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.7 KB | Display | ![]() |
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PDB format | ![]() | 62.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: ALA 20 - PRO 21 OMEGA ANGLE = 258.164 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: CIS PROLINE - PRO 140 / 3: CIS PROLINE - PRO 196 4: ASP 200 - PRO 201 OMEGA ANGLE = 115.757 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: RESIDUE PLP 409 IS BOUND TO LYS 258 FORMING A PROTONATED SCHIFF BASE LINKAGE BETWEEN NZ LYS 258 AND C4A PLP 409. | ||||||||
Details | THE MOLECULE IS A DIMER. TO GENERATE THE OTHER CHAIN ONE MUST APPLY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, 86.9-Y, 80.0-Z) TO THE COORDINATES IN THIS ENTRY. |
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Components
#1: Protein | ![]() Mass: 43619.215 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PLP / ![]() |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.61 % | |||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 7.5 / Method: vapor diffusion / Details: referred to J.Mol.Biol. 191.301-302 1986 | |||||||||||||||||||||||||
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 / Num. obs: 15069 / % possible obs: 72 % |
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Processing
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Refinement | Rfactor obs: 0.208 / Highest resolution: 2.4 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 5 Å / Num. reflection obs: 15069 / σ(I): 2 / Rfactor obs: 0.208 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 15 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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