1k75
From Proteopedia
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==Reference== | ==Reference== | ||
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[[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 15:04, 16 February 2009
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
Template:ABSTRACT PUBMED 11842181
About this Structure
1K75 is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- 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
Categories: 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
