1k75: Difference between revisions
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:11842181</ref><references group="xtra"/> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Histidinol dehydrogenase]] | [[Category: Histidinol dehydrogenase]] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:04:36 2009'' | ||
Revision as of 18:04, 16 February 2009
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
Template:ABSTRACT PUBMED 11842181
About this StructureAbout this Structure
1K75 is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:11842181 doi:10.1073/pnas.022476199
Page seeded by OCA on Mon Feb 16 17:04:36 2009
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Pages with broken file links
- Escherichia coli
- Histidinol dehydrogenase
- BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.
- Barbosa, J A.R G.
- Cygler, M.
- Larocque, R.
- Li, Y.
- Matte, A.
- Schrag, J.
- Sivaraman, J.
- 4 domain
- Bsgi
- Hisd
- Homodimer
- L-histidine biosynthesis
- L-histidinol dehydrogenase
- Montreal-kingston bacterial structural genomics initiative
- Nad cofactor
- Rossman fold
- Structural genomic
- Zinc