4a73: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
===SINGLE POINT MUTANT OF THERMUS THERMOPHILUS LACTATE DEHYDROGENASE=== | ===SINGLE POINT MUTANT OF THERMUS THERMOPHILUS LACTATE DEHYDROGENASE=== | ||
<!-- | |||
The line below this paragraph, {{ABSTRACT_PUBMED_22319152}}, adds the Publication Abstract to the page | |||
(as it appears on PubMed at http://www.pubmed.gov), where 22319152 is the PubMed ID number. | |||
--> | |||
{{ABSTRACT_PUBMED_22319152}} | |||
==About this Structure== | ==About this Structure== | ||
[[4a73]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xxe 2xxe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A73 OCA]. | [[4a73]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xxe 2xxe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A73 OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:022319152</ref><references group="xtra"/> | |||
[[Category: L-lactate dehydrogenase]] | [[Category: L-lactate dehydrogenase]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
Revision as of 09:22, 12 April 2012
SINGLE POINT MUTANT OF THERMUS THERMOPHILUS LACTATE DEHYDROGENASE
Template:ABSTRACT PUBMED 22319152
About this Structure
4a73 is a 4 chain structure with sequence from Thermus thermophilus. This structure supersedes the now removed PDB entry 2xxe. Full crystallographic information is available from OCA.
Reference
- Colletier JP, Aleksandrov A, Coquelle N, Mraihi S, Mendoza-Barbera E, Field M, Madern D. Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions. Mol Biol Evol. 2012 Jan 19. PMID:22319152 doi:10.1093/molbev/mss015
