4h2h

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{{STRUCTURE_4h2h| PDB=4h2h | SCENE= }}
{{STRUCTURE_4h2h| PDB=4h2h | SCENE= }}
===Crystal structure of an enolase (mandalate racemase subgroup, target EFI-502101) from Pelagibaca bermudensis htcc2601, with bound mg and l-4-hydroxyproline betaine (betonicine)===
===Crystal structure of an enolase (mandalate racemase subgroup, target EFI-502101) from Pelagibaca bermudensis htcc2601, with bound mg and l-4-hydroxyproline betaine (betonicine)===
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{{ABSTRACT_PUBMED_24056934}}
==About this Structure==
==About this Structure==
[[4h2h]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pelagibaca_bermudensis_htcc2601 Pelagibaca bermudensis htcc2601]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2H OCA].
[[4h2h]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pelagibaca_bermudensis_htcc2601 Pelagibaca bermudensis htcc2601]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2H OCA].
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==Reference==
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<ref group="xtra">PMID:024056934</ref><references group="xtra"/><references/>
[[Category: Pelagibaca bermudensis htcc2601]]
[[Category: Pelagibaca bermudensis htcc2601]]
[[Category: Almo, S C.]]
[[Category: Almo, S C.]]

Revision as of 05:56, 6 November 2013

Template:STRUCTURE 4h2h

Crystal structure of an enolase (mandalate racemase subgroup, target EFI-502101) from Pelagibaca bermudensis htcc2601, with bound mg and l-4-hydroxyproline betaine (betonicine)

Template:ABSTRACT PUBMED 24056934

About this Structure

4h2h is a 8 chain structure with sequence from Pelagibaca bermudensis htcc2601. Full crystallographic information is available from OCA.

Reference

  • Zhao S, Kumar R, Sakai A, Vetting MW, Wood BM, Brown S, Bonanno JB, Hillerich BS, Seidel RD, Babbitt PC, Almo SC, Sweedler JV, Gerlt JA, Cronan JE, Jacobson MP. Discovery of new enzymes and metabolic pathways by using structure and genome context. Nature. 2013 Sep 22. doi: 10.1038/nature12576. PMID:24056934 doi:http://dx.doi.org/10.1038/nature12576

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