[English] 日本語
![](img/lk-miru.gif)
- PDB-1maq: CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPA... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1maq | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE | ||||||
![]() | ASPARTATE AMINOTRANSFERASE | ||||||
![]() | AMINOTRANSFERASE | ||||||
Function / homology | ![]() Amino acid metabolism / Gluconeogenesis / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / aspartate metabolic process / glutamate metabolic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine:2-oxoglutarate aminotransferase activity / 2-oxoglutarate metabolic process / aspartate catabolic process ...Amino acid metabolism / Gluconeogenesis / kynurenine-oxoglutarate transaminase / kynurenine-oxoglutarate transaminase activity / aspartate metabolic process / glutamate metabolic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine:2-oxoglutarate aminotransferase activity / 2-oxoglutarate metabolic process / aspartate catabolic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / pyridoxal phosphate binding / mitochondrial matrix / protein homodimerization activity / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Malashkevich, V.N. / Jansonius, J.N. | ||||||
![]() | ![]() Title: Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Authors: Malashkevich, V.N. / Toney, M.D. / Jansonius, J.N. #1: ![]() Title: Structural Basis for Catalysis by Aspartate Aminotransferase Authors: Jansonius, J.N. / Vincent, M.G. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 99 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 74.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 447 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 461.2 KB | Display | |
Data in XML | ![]() | 11.5 KB | Display | |
Data in CIF | ![]() | 18.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO 138 / 2: CIS PROLINE - PRO 195 | ||||||||
Details | TWO-FOLD AXIS ALONG B RELATES SUBUNITS A AND B OF THE DIMER AND HENCE COORDINATES FOR SUBUNIT A ONLY ARE GIVEN. |
-
Components
#1: Protein | Mass: 44992.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
---|---|
#2: Chemical | ChemComp-PGU / |
#3: Water | ChemComp-HOH / |
Nonpolymer details | RESIDUE PGU 412 IS COMPOSED OF GLUTAMATE WITH THE COFACTOR PYRIDOXAL-5'-PHOSPHATE COVALENTLY BOUND ...RESIDUE PGU 412 IS COMPOSED OF GLUTAMATE WITH THE COFACTOR PYRIDOXAL-5'-PHOSPHATE COVALENTLY |
Sequence details | SEQUENCE ADVISORY NOTICE: DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: ...SEQUENCE ADVISORY NOTICE: DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.7 % | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | |||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 18083 / % possible obs: 90.2 % / Num. measured all: 43297 / Rmerge(I) obs: 0.062 |
-
Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→8 Å / σ(F): 0 /
| ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
| ||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||
Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 8 Å / Num. reflection all: 18083 / σ(F): 0 / Rfactor all: 0.169 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|