1olt
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_1olt| PDB=1olt | SCENE= }} | {{STRUCTURE_1olt| PDB=1olt | SCENE= }} | ||
- | + | ===COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.=== | |
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- | + | The line below this paragraph, {{ABSTRACT_PUBMED_14633981}}, adds the Publication Abstract to the page | |
+ | (as it appears on PubMed at http://www.pubmed.gov), where 14633981 is the PubMed ID number. | ||
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==About this Structure== | ==About this Structure== | ||
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[[Category: Radical sam enzyme]] | [[Category: Radical sam enzyme]] | ||
[[Category: S-adenosyl-l-methionine]] | [[Category: S-adenosyl-l-methionine]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
+ | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:21:07 2008'' |
Revision as of 17:21, 28 July 2008
COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME.
Template:ABSTRACT PUBMED 14633981
About this Structure
1OLT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes., Layer G, Moser J, Heinz DW, Jahn D, Schubert WD, EMBO J. 2003 Dec 1;22(23):6214-24. PMID:14633981
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