1rx4
From Proteopedia
(Difference between revisions)
m (Protected "1rx4" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
[[Image:1rx4.png|left|200px]] | [[Image:1rx4.png|left|200px]] | ||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_1rx4", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_1rx4| PDB=1rx4 | SCENE= }} | {{STRUCTURE_1rx4| PDB=1rx4 | SCENE= }} | ||
===DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE=== | ===DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE=== | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, {{ABSTRACT_PUBMED_9012674}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 9012674 is the PubMed ID number. | ||
| - | --> | ||
{{ABSTRACT_PUBMED_9012674}} | {{ABSTRACT_PUBMED_9012674}} | ||
| Line 22: | Line 11: | ||
==See Also== | ==See Also== | ||
| - | *[[Dihydrofolate reductase]] | + | *[[Dihydrofolate reductase|Dihydrofolate reductase]] |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:009012674</ref><ref group="xtra">PMID:010876245</ref><references group="xtra"/> |
[[Category: Dihydrofolate reductase]] | [[Category: Dihydrofolate reductase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
Revision as of 04:06, 27 July 2012
Contents |
DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
Template:ABSTRACT PUBMED 9012674
About this Structure
1rx4 is a 1 chain structure of Dihydrofolate reductase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Sawaya MR, Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 1997 Jan 21;36(3):586-603. PMID:9012674 doi:http://dx.doi.org/10.1021/bi962337c
- Iwakura M, Nakamura T, Yamane C, Maki K. Systematic circular permutation of an entire protein reveals essential folding elements. Nat Struct Biol. 2000 Jul;7(7):580-5. PMID:10876245 doi:10.1038/76811
