4eou
From Proteopedia
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===Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site=== | ===Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site=== | ||
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+ | (as it appears on PubMed at http://www.pubmed.gov), where 22552955 is the PubMed ID number. | ||
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==About this Structure== | ==About this Structure== | ||
[[4eou]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ubs 3ubs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOU OCA]. | [[4eou]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ubs 3ubs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOU OCA]. | ||
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:022552955</ref><references group="xtra"/> | ||
[[Category: Dihydrodipicolinate synthase]] | [[Category: Dihydrodipicolinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] |
Revision as of 06:55, 6 June 2012
Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site
Template:ABSTRACT PUBMED 22552955
About this Structure
4eou is a 2 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 3ubs. Full crystallographic information is available from OCA.
Reference
- Boughton BA, Dobson RC, Hutton CA. The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semi-aldehyde: Unambiguous resolution of the stereochemistry of the condensation product. Proteins. 2012 May 2. doi: 10.1002/prot.24106. PMID:22552955 doi:10.1002/prot.24106