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IF

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Structure paper

TitleWhat Makes a Protein Fold Amenable to Functional Innovation? Fold Polarity and Stability Trade-offs.
Journal, issue, pagesJ. Mol. Biol., Vol. 425, Page 2609-2621, Year 2013
Publish dateDec 9, 2012 (structure data deposition date)
AuthorsDellus-Gur, E. / Toth-Petroczy, A. / Elias, M. / Tawfik, D.S.
External linksJ. Mol. Biol. / PubMed:23542341
MethodsX-ray diffraction
Resolution2.2 - 2.68 Å
Structure data

PDB-4ibr:
Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S/E104K mutations
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-4ibx:
Crystal structure of stabilized TEM-1 beta-lactamase variant v.13
Method: X-RAY DIFFRACTION / Resolution: 2.68 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / beta-lactamase / TEM-1 beta-lactamase

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