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- PDB-7aat: X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOC... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7aat | ||||||
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Title | X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE | ||||||
![]() | ASPARTATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE(AMINOTRANSFERASE) | ||||||
Function / homology | ![]() Amino acid metabolism / Gluconeogenesis / aspartate catabolic process / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / aspartate metabolic process / glutamate metabolic process / 2-oxoglutarate metabolic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity ...Amino acid metabolism / Gluconeogenesis / aspartate catabolic process / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / aspartate metabolic process / glutamate metabolic process / 2-oxoglutarate metabolic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / biosynthetic process / pyridoxal phosphate binding / mitochondrial matrix / protein homodimerization activity / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Mcphalen, C.A. / Vincent, M.G. / Jansonius, J.N. | ||||||
![]() | ![]() Title: X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. Authors: McPhalen, C.A. / Vincent, M.G. / Jansonius, J.N. #1: ![]() Title: The Open(Slash)Closed Conformational Equilibrium of Aspartate Aminotransferase: Studies in the Crystalline State and with a Fluorescent Probe in Solution Authors: Picot, D. / Sandmeier, E. / Thaller, C. / Vincent, M.G. / Christen, P. / Jansonius, J.N. #2: ![]() Title: Mechanism of Action of Aspartate Aminotransferase Proposed on the Basis of its Spatial Structure Authors: Kirsch, J.F. / Eichele, G. / Ford, G.C. / Vincent, M.G. / Jansonius, J.N. / Gehring, H. / Christen, P. #3: ![]() Title: Three-Dimensional Structure of a Pyridoxal-Phosphate-Dependent Enzyme, Mitochondrial Aspartate Aminotransferase Authors: Ford, G.C. / Eichele, G. / Jansonius, J.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 177.7 KB | Display | ![]() |
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PDB format | ![]() | 146.3 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: CIS PROLINE - PRO A 138 / 2: CIS PROLINE - PRO A 195 / 3: CIS PROLINE - PRO B 138 / 4: CIS PROLINE - PRO B 195 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.92423, 0.34441, -0.16487), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*, WITH AN RMSD=0.66. THE MOLECULE IS AN ALPHA2 DIMER. THE SUBUNITS ARE RELATED BY A LOCAL TWO-FOLD ROTATION AXIS. THEY ARE DISTINGUISHED BY CHAIN IDENTIFIERS A AND B, RESPECTIVELY. THE RESIDUES IN EACH SUBUNIT ARE NUMBERED FROM 3 TO 410, ACCORDING TO A SEQUENCE ALIGNMENT WITH THE LONGER SEQUENCE OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE (SEE U. GRAF-HAUSNER, K.J. WILSON AND P. CHRISTEN (1983). J.BIOL.CHEM. 258, 8813-8826). | |
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Components
#1: Protein | Mass: 44992.484 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Nonpolymer details | ONE MOLECULE OF THE COFACTOR PYRIDOXAL-5'-PHOSPHATE (PLP) IS BOUND PER SUBUNIT THROUGH A SCHIFF ...ONE MOLECULE OF THE COFACTOR PYRIDOXAL-5'-PHOSPHATE (PLP) IS BOUND PER SUBUNIT THROUGH A SCHIFF BASE (ALDIMINE) DOUBLE BOND TO LYS 258 OF THAT SUBUNIT. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.39 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 60850 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 10 Å / Num. reflection all: 60850 / σ(F): 0 / Rfactor all: 0.166 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 0.029 |