6dfr
From Proteopedia
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===CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE=== | ===CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[6dfr]] is a 1 chain structure of [[Dihydrofolate reductase]] 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=6DFR OCA]. | |
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| + | ==See Also== | ||
| + | *[[Dihydrofolate reductase|Dihydrofolate reductase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:002185835</ref><references group="xtra"/> |
[[Category: Dihydrofolate reductase]] | [[Category: Dihydrofolate reductase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Oatley, S J.]] | [[Category: Oatley, S J.]] | ||
[[Category: Oxido-reductase]] | [[Category: Oxido-reductase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:43:56 2009'' | ||
Revision as of 22:07, 25 July 2012
Contents |
CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE
Template:ABSTRACT PUBMED 2185835
About this Structure
6dfr is a 1 chain structure of Dihydrofolate reductase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Bystroff C, Oatley SJ, Kraut J. Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry. 1990 Apr 3;29(13):3263-77. PMID:2185835
