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3dl5
From Proteopedia
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| + | [[Image:3dl5.jpg|left|200px]] | ||
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| + | {{STRUCTURE_3dl5| PDB=3dl5 | SCENE= }} | ||
| - | + | ===Crystal Structure of the A287F Active Site Mutant of TS-DHFR from Cryptosporidium hominis=== | |
| - | Description: Crystal Structure of the A287F Active Site Mutant of TS-DHFR from Cryptosporidium hominis | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18672899}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 18672899 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_18672899}} | ||
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| + | ==About this Structure== | ||
| + | 3DL5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL5 OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase., Martucci WE, Vargo MA, Anderson KS, Biochemistry. 2008 Aug 26;47(34):8902-11. Epub 2008 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18672899 18672899] | ||
| + | [[Category: Cryptosporidium hominis]] | ||
| + | [[Category: Dihydrofolate reductase]] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Anderson, K S.]] | ||
| + | [[Category: Martucci, W E.]] | ||
| + | [[Category: Vargo, M A.]] | ||
| + | [[Category: Enzyme active site mutant]] | ||
| + | [[Category: Enzyme-ligand complex]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 20 12:06:56 2008'' | ||
Revision as of 09:06, 20 August 2008
Crystal Structure of the A287F Active Site Mutant of TS-DHFR from Cryptosporidium hominis
Template:ABSTRACT PUBMED 18672899
About this Structure
3DL5 is a Single protein structure of sequence from Cryptosporidium hominis. Full crystallographic information is available from OCA.
Reference
Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase., Martucci WE, Vargo MA, Anderson KS, Biochemistry. 2008 Aug 26;47(34):8902-11. Epub 2008 Aug 2. PMID:18672899
Page seeded by OCA on Wed Aug 20 12:06:56 2008
