2hmf
From Proteopedia
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|PDB= 2hmf |SIZE=350|CAPTION= <scene name='initialview01'>2hmf</scene>, resolution 2.700Å | |PDB= 2hmf |SIZE=350|CAPTION= <scene name='initialview01'>2hmf</scene>, resolution 2.700Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2cdq|2CDQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmf OCA], [http://www.ebi.ac.uk/pdbsum/2hmf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hmf RCSB]</span> | ||
}} | }} | ||
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[[Category: Faehnle, C R.]] | [[Category: Faehnle, C R.]] | ||
[[Category: Viola, R E.]] | [[Category: Viola, R E.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: ASP]] | ||
| - | [[Category: MG]] | ||
[[Category: aspartokinase]] | [[Category: aspartokinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:32:18 2008'' |
Revision as of 00:32, 31 March 2008
| |||||||
| , resolution 2.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Aspartate kinase, with EC number 2.7.2.4 | ||||||
| Related: | 2CDQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate
Overview
The activation of the beta-carboxyl group of aspartate catalyzed by aspartokinase is the commitment step to amino-acid biosynthesis in the aspartate pathway. The first structure of a microbial aspartokinase, that from Methanococcus jannaschii, has been determined in the presence of the amino-acid substrate L-aspartic acid and the nucleotide product MgADP. The enzyme assembles into a dimer of dimers, with the interfaces mediated by both the N- and C-terminal domains. The active-site functional groups responsible for substrate binding and specificity have been identified and roles have been proposed for putative catalytic functional groups.
About this Structure
2HMF is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase., Faehnle CR, Liu X, Pavlovsky A, Viola RE, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):962-6. Epub 2006 Sep 30. PMID:17012784
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