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- PDB-2aat: 2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2aat | ||||||
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Title | 2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI | ||||||
![]() | ASPARTATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE(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 | ![]() | ||||||
![]() | Smith, D. / Almo, S.C. / Toney, M. / Ringe, D. | ||||||
![]() | ![]() Title: 2.8-A-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. #1: ![]() 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 | ![]() | 84.6 KB | Display | ![]() |
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PDB format | ![]() | 56.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 404.1 KB | Display | ![]() |
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Full document | ![]() | 509.4 KB | Display | |
Data in XML | ![]() | 23.5 KB | Display | |
Data in CIF | ![]() | 32.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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 140 AND 196 ARE CIS PROLINES. | ||||||||
Details | THE MOLECULE IS A DIMER. TO GENERATE THE OTHER CHAIN ONE MUST APPLY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, 86.74-Y, 79.84-Z) TO THE COORDINATES IN THIS ENTRY. |
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Components
#1: Protein | Mass: 43561.109 Da / Num. of mol.: 1 / Mutation: K246A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-PMP / |
Sequence details | THE RESIDUE NUMBERING USED IN THIS ENTRY HAS BEEN CHOSEN TO MAXIMIZE HOMOLOGY BETWEEN E. COLI ...THE RESIDUE NUMBERING USED IN THIS ENTRY HAS BEEN CHOSEN TO MAXIMIZE HOMOLOGY BETWEEN E. COLI AATASE AND CHICKEN MITOCHONDR |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.11 Å3/Da / Density % sol: 60.51 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: batch method | ||||||||||||||||||||
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: 2.8 Å / Num. obs: 8783 / % possible obs: 64 % |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.8→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 10 Å / Num. reflection obs: 8433 / Rfactor obs: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 14 Å2 |