1emj: Difference between revisions
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[[Image:1emj.png|left|200px]] | [[Image:1emj.png|left|200px]] | ||
{{STRUCTURE_1emj| PDB=1emj | SCENE= }} | {{STRUCTURE_1emj| PDB=1emj | SCENE= }} | ||
===URACIL-DNA GLYCOSYLASE BOUND TO DNA CONTAINING A 4'-THIO-2'DEOXYURIDINE ANALOG PRODUCT=== | ===URACIL-DNA GLYCOSYLASE BOUND TO DNA CONTAINING A 4'-THIO-2'DEOXYURIDINE ANALOG PRODUCT=== | ||
{{ABSTRACT_PUBMED_10805771}} | {{ABSTRACT_PUBMED_10805771}} | ||
==About this Structure== | ==About this Structure== | ||
[[1emj]] is a 3 chain structure of [[DNA glycosylate]] with 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=1EMJ OCA]. | |||
==See Also== | |||
*[[DNA glycosylate|DNA glycosylate]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:010805771</ref><ref group="xtra">PMID:010926503</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Uridine nucleosidase]] | [[Category: Uridine nucleosidase]] | ||
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[[Category: Walcher, G.]] | [[Category: Walcher, G.]] | ||
[[Category: Alpha/beta fold]] | [[Category: Alpha/beta fold]] | ||
[[Category: Hydrolase-dna complex]] | |||
[[Category: Protein/dna]] | [[Category: Protein/dna]] | ||
[[Category: Uracil-dna glycosylase]] | [[Category: Uracil-dna glycosylase]] | ||
Revision as of 01:53, 26 July 2012
URACIL-DNA GLYCOSYLASE BOUND TO DNA CONTAINING A 4'-THIO-2'DEOXYURIDINE ANALOG PRODUCTURACIL-DNA GLYCOSYLASE BOUND TO DNA CONTAINING A 4'-THIO-2'DEOXYURIDINE ANALOG PRODUCT
Template:ABSTRACT PUBMED 10805771
About this StructureAbout this Structure
1emj is a 3 chain structure of DNA glycosylate with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Parikh SS, Walcher G, Jones GD, Slupphaug G, Krokan HE, Blackburn GM, Tainer JA. Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5083-8. PMID:10805771
- ↑ Grzesiak A, Helland R, Smalas AO, Krowarsch D, Dadlez M, Otlewski J. Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases. J Mol Biol. 2000 Aug 4;301(1):205-17. PMID:10926503 doi:10.1006/jmbi.2000.3935