1ksp
From Proteopedia
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[[Image:1ksp.png|left|200px]] | [[Image:1ksp.png|left|200px]] | ||
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{{STRUCTURE_1ksp| PDB=1ksp | SCENE= }} | {{STRUCTURE_1ksp| PDB=1ksp | SCENE= }} | ||
- | ===DNA | + | ===DNA polymerase I Klenow fragment (E.C.2.7.7.7) mutant/DNA complex=== |
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{{ABSTRACT_PUBMED_9514742}} | {{ABSTRACT_PUBMED_9514742}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[1ksp]] is a 2 chain structure of [[DNA polymerase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSP OCA]. | |
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+ | ==See Also== | ||
+ | *[[DNA polymerase|DNA polymerase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:009514742</ref><ref group="xtra">PMID:015048824</ref><references group="xtra"/> |
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: C A. | + | [[Category: Brautigam, C A.]] |
+ | [[Category: Steitz, T A.]] | ||
[[Category: Exonuclease]] | [[Category: Exonuclease]] | ||
[[Category: Phosphorothioate]] | [[Category: Phosphorothioate]] | ||
- | [[Category: Transferase | + | [[Category: Transferase-dna complex]] |
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Revision as of 03:31, 27 July 2012
Contents |
DNA polymerase I Klenow fragment (E.C.2.7.7.7) mutant/DNA complex
Template:ABSTRACT PUBMED 9514742
About this Structure
1ksp is a 2 chain structure of DNA polymerase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Brautigam CA, Steitz TA. Structural principles for the inhibition of the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates. J Mol Biol. 1998 Mar 27;277(2):363-77. PMID:9514742 doi:http://dx.doi.org/10.1006/jmbi.1997.1586
- Hicks JM, Hsu VL. The extended left-handed helix: a simple nucleic acid-binding motif. Proteins. 2004 May 1;55(2):330-8. PMID:15048824 doi:10.1002/prot.10630