000 01380 a2200385 4500
005 20250515051235.0
264 0 _c20070320
008 200703s 0 0 eng d
022 _a0022-2836
024 7 _a10.1016/j.jmb.2006.11.027
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aOelschlaeger, Peter
245 0 0 _aHydroxyl groups in the betabeta sandwich of metallo-beta-lactamases favor enzyme activity: Tyr218 and Ser262 pull down the lid.
_h[electronic resource]
260 _bJournal of molecular biology
_cFeb 2007
300 _a316-29 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aCatalysis
650 0 4 _aComputer Simulation
650 0 4 _aEnzyme Activation
650 0 4 _aHydrogen Bonding
650 0 4 _aHydroxides
_xchemistry
650 0 4 _aMetals
_xchemistry
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Structure
650 0 4 _aMutation
650 0 4 _aProtein Structure, Tertiary
650 0 4 _aSerine
_xchemistry
650 0 4 _aStructure-Activity Relationship
650 0 4 _aTyrosine
_xchemistry
650 0 4 _aZinc
_xchemistry
650 0 4 _abeta-Lactamases
_xchemistry
700 1 _aPleiss, Juergen
773 0 _tJournal of molecular biology
_gvol. 366
_gno. 1
_gp. 316-29
856 4 0 _uhttps://doi.org/10.1016/j.jmb.2006.11.027
_zAvailable from publisher's website
999 _c16726734
_d16726734