1m15: Difference between revisions
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|PDB= 1m15 |SIZE=350|CAPTION= <scene name='initialview01'>1m15</scene>, resolution 1.20Å | |PDB= 1m15 |SIZE=350|CAPTION= <scene name='initialview01'>1m15</scene>, resolution 1.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3. 2.7.3.3.] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3. 2.7.3.3.] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m15 OCA], [http://www.ebi.ac.uk/pdbsum/1m15 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m15 RCSB]</span> | |||
}} | }} | ||
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[[Category: Somasundaram, T.]] | [[Category: Somasundaram, T.]] | ||
[[Category: Yousef, M S.]] | [[Category: Yousef, M S.]] | ||
[[Category: adenosine triphosphate]] | [[Category: adenosine triphosphate]] | ||
[[Category: arginine kinase]] | [[Category: arginine kinase]] | ||
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[[Category: transition state analog]] | [[Category: transition state analog]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:09:55 2008'' | ||
Revision as of 22:09, 30 March 2008
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| , resolution 1.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Transferase, with EC number 2.7.3.3. | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TRANSITION STATE STRUCTURE OF ARGININE KINASE
OverviewOverview
The three-dimensional crystal structure of an arginine kinase transition-state analogue complex has been refined at 1.2 A resolution, with an overall R factor of 12.3%. The current model provides a unique opportunity to analyze the structure of a bimolecular (phosphagen kinase) enzyme in its transition state. This atomic resolution structure confirms in-line transfer of the phosphoryl group and the catalytic importance of the precise alignment of the substrates. The structure is consistent with a concerted proton transfer that has been proposed for an unrelated kinase. Refinement of anisotropic temperature factors and translation-libration-screw (TLS) analyses led to the identification of four rigid groups and their prevalent modes of motion in the transition state. The relative magnitudes of the mobility of rigid groups are consistent with their proposed roles in catalysis.
About this StructureAbout this Structure
1M15 is a Single protein structure of sequence from Limulus polyphemus. Full crystallographic information is available from OCA.
ReferenceReference
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights., Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2009-17. Epub 2002, Nov 23. PMID:12454458
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