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- PDB-1asa: THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F)... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1asa | ||||||
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Title | THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE | ||||||
![]() | ASPARTATE AMINOTRANSFERASE | ||||||
![]() | AMINOTRANSFERASE | ||||||
Function / homology | ![]() L-phenylalanine biosynthetic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine-2-oxoglutarate transaminase activity / aspartate catabolic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / pyridoxal phosphate binding / protein homodimerization activity / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schumacher, C. / Ringe, D. | ||||||
![]() | ![]() Title: The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase Authors: Schumacher, C. / Ringe, D. #1: ![]() 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. #2: ![]() 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. #3: ![]() 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 | ![]() | 83.8 KB | Display | ![]() |
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PDB format | ![]() | 63 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 397.9 KB | Display | ![]() |
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Full document | ![]() | 412.5 KB | Display | |
Data in XML | ![]() | 10.8 KB | Display | |
Data in CIF | ![]() | 15.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 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. |
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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: Chemical | ChemComp-MAE / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | HET GROUP PLP 258 IS BOUND TO LYS 258 FORMING A PROTONATED SCHIFF BASE LINKAGE (BETWEEN NZ LYS 258 ...HET GROUP PLP 258 IS BOUND TO LYS 258 FORMING A PROTONATED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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 |
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Processing
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Refinement | Rfactor Rwork: 0.198 / Rfactor obs: 0.198 / 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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