2cet
From Proteopedia
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|PDB= 2cet |SIZE=350|CAPTION= <scene name='initialview01'>2cet</scene>, resolution 1.97Å | |PDB= 2cet |SIZE=350|CAPTION= <scene name='initialview01'>2cet</scene>, resolution 1.97Å | ||
|SITE= <scene name='pdbsite=NUC:Pgi+Binding+Site+For+Chain+B'>NUC</scene> | |SITE= <scene name='pdbsite=NUC:Pgi+Binding+Site+For+Chain+B'>NUC</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGI:(5R,6R,7S,8S)-5-(HYDROXYMETHYL)-2-(2-PHENYLETHYL)-1,5,6,7,8,8A-HEXAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL'>PGI</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cet OCA], [http://www.ebi.ac.uk/pdbsum/2cet PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cet RCSB]</span> | ||
}} | }} | ||
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[[Category: Roberts, S.]] | [[Category: Roberts, S.]] | ||
[[Category: Vasella, A.]] | [[Category: Vasella, A.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: PGI]] | ||
[[Category: family 1]] | [[Category: family 1]] | ||
[[Category: glycoside hydrolase]] | [[Category: glycoside hydrolase]] | ||
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[[Category: transition state mimic]] | [[Category: transition state mimic]] | ||
| - | ''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 02:20:30 2008'' |
Revision as of 23:20, 30 March 2008
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| , resolution 1.97Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Beta-glucosidase, with EC number 3.2.1.21 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH PHENETHYL-SUBSTITUTED GLUCOIMIDAZOLE
Overview
Inhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound.
About this Structure
2CET is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors., Gloster TM, Roberts S, Perugino G, Rossi M, Moracci M, Panday N, Terinek M, Vasella A, Davies GJ, Biochemistry. 2006 Oct 3;45(39):11879-84. PMID:17002288
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