1bx4
From Proteopedia
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|PDB= 1bx4 |SIZE=350|CAPTION= <scene name='initialview01'>1bx4</scene>, resolution 1.50Å | |PDB= 1bx4 |SIZE=350|CAPTION= <scene name='initialview01'>1bx4</scene>, resolution 1.50Å | ||
|SITE= <scene name='pdbsite=ADA:Adn+350+Binds+In+The+Substrate+Binding+Site'>ADA</scene> and <scene name='pdbsite=ADB:Adn+355+Binds+In+The+Atp+Binding+Site'>ADB</scene> | |SITE= <scene name='pdbsite=ADA:Adn+350+Binds+In+The+Substrate+Binding+Site'>ADA</scene> and <scene name='pdbsite=ADB:Adn+355+Binds+In+The+Atp+Binding+Site'>ADB</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bx4 OCA], [http://www.ebi.ac.uk/pdbsum/1bx4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bx4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Erion, M D.]] | [[Category: Erion, M D.]] | ||
[[Category: Mathews, I I.]] | [[Category: Mathews, I I.]] | ||
| - | [[Category: ADN]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MG]] | ||
[[Category: human adenosine kinase]] | [[Category: human adenosine kinase]] | ||
| - | ''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 19:10:05 2008'' |
Revision as of 16:10, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , | ||||||
| Activity: | Adenosine kinase, with EC number 2.7.1.20 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS
Overview
Adenosine kinase (AK) is a key enzyme in the regulation of extracellular adenosine and intracellular adenylate levels. Inhibitors of adenosine kinase elevate adenosine to levels that activate nearby adenosine receptors and produce a wide variety of therapeutically beneficial activities. Accordingly, AK is a promising target for new analgesic, neuroprotective, and cardioprotective agents. We determined the structure of human adenosine kinase by X-ray crystallography using MAD phasing techniques and refined the structure to 1.5 A resolution. The enzyme structure consisted of one large alpha/beta domain with nine beta-strands, eight alpha-helices, and one small alpha/beta-domain with five beta-strands and two alpha-helices. The active site is formed along the edge of the beta-sheet in the large domain while the small domain acts as a lid to cover the upper face of the active site. The overall structure is similar to the recently reported structure of ribokinase from Escherichia coli [Sigrell et al. (1998) Structure 6, 183-193]. The structure of ribokinase was determined at 1.8 A resolution and represents the first structure of a new family of carbohydrate kinases. Two molecules of adenosine were present in the AK crystal structure with one adenosine molecule located in a site that matches the ribose site in ribokinase and probably represents the substrate-binding site. The second adenosine site overlaps the ADP site in ribokinase and probably represents the ATP site. A Mg2+ ion binding site is observed in a trough between the two adenosine sites. The structure of the active site is consistent with the observed substrate specificity. The active-site model suggests that Asp300 is an important catalytic residue involved in the deprotonation of the 5'-hydroxyl during the phosphate transfer.
About this Structure
1BX4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human adenosine kinase at 1.5 A resolution., Mathews II, Erion MD, Ealick SE, Biochemistry. 1998 Nov 10;37(45):15607-20. PMID:9843365
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