1ivr
From Proteopedia
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|PDB= 1ivr |SIZE=350|CAPTION= <scene name='initialview01'>1ivr</scene>, resolution 2.4Å | |PDB= 1ivr |SIZE=350|CAPTION= <scene name='initialview01'>1ivr</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CBA:N-PYRIDOXYL-2,3-DIHYDROXYASPARTIC ACID-5-MONOPHOSPHATE'>CBA</scene> | + | |LIGAND= <scene name='pdbligand=CBA:N-PYRIDOXYL-2,3-DIHYDROXYASPARTIC+ACID-5-MONOPHOSPHATE'>CBA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ivr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivr OCA], [http://www.ebi.ac.uk/pdbsum/1ivr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ivr RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Stosch, A Graf Von.]] | [[Category: Stosch, A Graf Von.]] | ||
| - | [[Category: CBA]] | ||
[[Category: aspartate aminotransferase]] | [[Category: aspartate aminotransferase]] | ||
[[Category: carbinolamine]] | [[Category: carbinolamine]] | ||
[[Category: erythro-beta-hydroxyaspartate]] | [[Category: erythro-beta-hydroxyaspartate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:18 2008'' |
Revision as of 18:25, 30 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF ASPARTATE AMINOTRANSFERASE
Overview
The crystal structure of mitochondrial aspartate aminotransferase (mAAT) of chicken complexed with erythro-beta-hydroxyaspartate has been determined at 2.4 A resolution. Pregrown crystals of mAAT complexed with the inhibitor maleate (closed enzyme conformation, orthorhombic space group C222(1)) were soaked in solutions of erythro-beta-hydroxyaspartate. The ligand exchange was monitored by microspectrophotometry. The active site turned out to be predominantly occupied by the carbinolamine intermediate. The carbinolamine is a true intermediate of the catalytic cycle forming the last covalently bound enzyme:substrate complex before release of the keto acid product. Occupancies of approximately 80% for the carbinolamine and of approximately 20% for the quinonoid intermediate were obtained. Two hydrogen bonds were identified that are potentially relevant for the accumulation of the carbinolamine intermediate: one to the hydroxyl group of Tyr 70* and the other to the epsilon-NH2 group of Lys 258.
About this Structure
1IVR is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate., von Stosch AG, Biochemistry. 1996 Dec 3;35(48):15260-8. PMID:8952476
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