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- PDB-3aat: ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3aat | ||||||
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Title | ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE | ||||||
![]() | ASPARTATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE(AMINOTRANSFERASE) | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Danishefsky, A.T. / Ringe, D. / Petsko, G.A. | ||||||
![]() | ![]() 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. #1: ![]() Title: 2.8-Angstroms-Resolution Crystal Structure of an Active-Site Mutant of Aspartate Aminotransferse from Escherichia Coli Authors: Smith, D.L. / Almo, S.C. / Toney, M.D. / Ringe, D. #2: ![]() Title: Preliminary X-Ray Data for Aspartate Aminotransferase from Escherichia Coli Authors: Smith, D.L. / Ringe, D. / Finlayson, W.L. / Kirsch, J.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 84.1 KB | Display | ![]() |
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PDB format | ![]() | 58.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar 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: RESIDUES 138 AND 195 ARE CIS PROLINES. | ||||||||
Details | THE MOLECULE IS A DIMER. TO GENERATE THE OTHER CHAIN ONE MUST APPLY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, 87.60-Y, 78.80-Z) TO THE COORDINATES IN THIS ENTRY. |
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Components
#1: Protein | Mass: 43609.191 Da / Num. of mol.: 1 / Mutation: R374F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-PLP / |
Sequence details | THE RESIDUE NUMBERING USED IN THIS ENTRY HAS BEEN CHOSEN TO MAXIMIZE HOMOLOGY WITH OTHER SPECIES OF ...THE RESIDUE NUMBERING USED IN THIS ENTRY HAS BEEN CHOSEN TO MAXIMIZE HOMOLOGY WITH OTHER SPECIES OF THE ENZYME. THEREFORE, THE RESIDUE NUMBERING STARTS WITH 5 AND RESIDUE NUMBERS 128 - 132, 153, 232, AND 407 HAVE NOT BEEN USED. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.09 Å3/Da / Density % sol: 60.14 % | |||||||||||||||
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Crystal grow | *PLUS 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: 2.5 Å / Rmerge(I) obs: 0.067 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.8→10 Å / Rfactor obs: 0.215 Details: THE GEOMETRY AT MANY OF THE COIL REGIONS WAS NOT CLEARLY DEFINED IN THE ELECTRON DENSITY MAPS. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 10 Å / Num. reflection obs: 10531 / σ(I): 1 / Rfactor obs: 0.215 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 12 Å2 |