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1brm
From Proteopedia
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{{STRUCTURE_1brm| PDB=1brm | SCENE= }} | {{STRUCTURE_1brm| PDB=1brm | SCENE= }} | ||
===ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI=== | ===ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI=== | ||
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{{ABSTRACT_PUBMED_10369777}} | {{ABSTRACT_PUBMED_10369777}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1brm]] is a 3 chain structure of [[Aspartate-semialdehyde dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRM OCA]. | |
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| + | ==See Also== | ||
| + | *[[Aspartate-semialdehyde dehydrogenase|Aspartate-semialdehyde dehydrogenase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:010369777</ref><ref group="xtra">PMID:008605178</ref><references group="xtra"/> |
[[Category: Aspartate-semialdehyde dehydrogenase]] | [[Category: Aspartate-semialdehyde dehydrogenase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Viola, R E.]] | [[Category: Viola, R E.]] | ||
| - | [[Category: Crystal structure]] | ||
[[Category: Dehydrogenase]] | [[Category: Dehydrogenase]] | ||
[[Category: Enzyme]] | [[Category: Enzyme]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Nadp]] | [[Category: Nadp]] | ||
| - | + | [[Category: Oxidoreductase]] | |
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Revision as of 08:31, 26 July 2012
Contents |
ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI
Template:ABSTRACT PUBMED 10369777
About this Structure
1brm is a 3 chain structure of Aspartate-semialdehyde dehydrogenase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J Mol Biol. 1999 Jun 18;289(4):991-1002. PMID:10369777 doi:10.1006/jmbi.1999.2828
- Buckle AM, Cramer P, Fersht AR. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry. 1996 Apr 9;35(14):4298-305. PMID:8605178 doi:http://dx.doi.org/10.1021/bi9524676
