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Open data
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Basic information
Entry | Database: PDB / ID: 5eaa | ||||||
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Title | ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION | ||||||
![]() | 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 | ![]() | ||||||
![]() | Jeffery, C.J. / Gloss, L.M. / Petsko, G.A. / Ringe, D. | ||||||
![]() | ![]() Title: The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Authors: Jeffery, C.J. / Gloss, L.M. / Petsko, G.A. / 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 | ![]() | 87.2 KB | Display | ![]() |
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PDB format | ![]() | 69.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 387.9 KB | Display | ![]() |
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Full document | ![]() | 401.8 KB | Display | |
Data in XML | ![]() | 11 KB | Display | |
Data in CIF | ![]() | 16.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1b4xC ![]() 1qirC ![]() 1qisC ![]() 1qitC ![]() 1asaS S: Starting model for refinement C: citing same article ( |
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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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Components
#1: Protein | Mass: 43603.148 Da / Num. of mol.: 1 / Fragment: COMPLETE SUBUNIT / Mutation: YES Source method: isolated from a genetically manipulated source Details: PYRIDOXAL PHOSPHATE COFACTOR COVALENTLY BOUND TO LYS 258 VIA SCHIFF BASE LINKAGE 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: 3.1 Å3/Da / Density % sol: 60 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.50 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 297 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 19539 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 1 % / Rmerge(I) obs: 0.059 |
Reflection shell | Highest resolution: 2.4 Å |
Reflection | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 50 Å / Observed criterion σ(I): 0 / Redundancy: 1 % / Rmerge(I) obs: 0.072 |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: 1ASA Resolution: 2.4→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 22.46 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PARHCSDX.PRO / Topol file: TOPHCSDX.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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