3eos
From Proteopedia
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[[Image:3eos.png|left|200px]] | [[Image:3eos.png|left|200px]] | ||
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{{STRUCTURE_3eos| PDB=3eos | SCENE= }} | {{STRUCTURE_3eos| PDB=3eos | SCENE= }} | ||
===tRNA-guanine transglycosylase in complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one=== | ===tRNA-guanine transglycosylase in complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3eos]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EOS OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019894214</ref><references group="xtra"/> |
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[[Category: Zymomonas mobilis]] | [[Category: Zymomonas mobilis]] | ||
| + | [[Category: TRNA-guanine transglycosylase]] | ||
[[Category: Heine, A.]] | [[Category: Heine, A.]] | ||
[[Category: Klebe, G.]] | [[Category: Klebe, G.]] | ||
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[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Trna processing]] | [[Category: Trna processing]] | ||
| - | [[Category: Zinc]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 9 14:00:05 2009'' | ||
Revision as of 13:40, 6 February 2013
tRNA-guanine transglycosylase in complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Template:ABSTRACT PUBMED 19894214
About this Structure
3eos is a 1 chain structure with sequence from Zymomonas mobilis. Full crystallographic information is available from OCA.
Reference
- Ritschel T, Kohler PC, Neudert G, Heine A, Diederich F, Klebe G. How to Replace the Residual Solvation Shell of Polar Active Site Residues to Achieve Nanomolar Inhibition of tRNA-Guanine Transglycosylase. ChemMedChem. 2009 Dec;4(12):2012-23. PMID:19894214 doi:10.1002/cmdc.200900343
