1bx4
From Proteopedia
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| - | [[Image:1bx4.gif|left|200px]] | + | [[Image:1bx4.gif|left|200px]] |
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| - | '''STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADN:ADENOSINE'>ADN</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BX4 is a [ | + | 1BX4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9843365 9843365] |
[[Category: Adenosine kinase]] | [[Category: Adenosine kinase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: human adenosine kinase]] | [[Category: human adenosine kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:16:54 2008'' |
Revision as of 08:16, 20 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , and | ||||||
| Activity: | Adenosine kinase, with EC number 2.7.1.20 | ||||||
| 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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