000 | 01964 a2200553 4500 | ||
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005 | 20250514074736.0 | ||
264 | 0 | _c20040414 | |
008 | 200404s 0 0 eng d | ||
022 | _a0969-2126 | ||
024 | 7 |
_a10.1016/s0969-2126(03)00154-0 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aKang, Lin-Woo | |
245 | 0 | 0 |
_aStructure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis. _h[electronic resource] |
260 |
_bStructure (London, England : 1993) _cAug 2003 |
||
300 |
_a1015-23 p. _bdigital |
||
500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 |
_aAdenosine Diphosphate Ribose _xmetabolism |
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aCatalysis |
650 | 0 | 4 | _aCrystallography, X-Ray |
650 | 0 | 4 | _aDimerization |
650 | 0 | 4 | _aEnzyme Activation |
650 | 0 | 4 |
_aEscherichia coli _xenzymology |
650 | 0 | 4 |
_aGadolinium _xmetabolism |
650 | 0 | 4 | _aHelix-Loop-Helix Motifs |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 | _aHydrogen Bonding |
650 | 0 | 4 |
_aHydrolases _xchemistry |
650 | 0 | 4 | _aLigands |
650 | 0 | 4 |
_aManganese _xmetabolism |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aMolecular Structure |
650 | 0 | 4 |
_aMycobacterium tuberculosis _xenzymology |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 |
_aPyrophosphatases _xchemistry |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 | _aSpecies Specificity |
650 | 0 | 4 | _aSubstrate Specificity |
650 | 0 | 4 |
_aWater _xchemistry |
700 | 1 | _aGabelli, Sandra B | |
700 | 1 | _aCunningham, Jennifer E | |
700 | 1 | _aO'Handley, Suzanne F | |
700 | 1 | _aAmzel, L Mario | |
773 | 0 |
_tStructure (London, England : 1993) _gvol. 11 _gno. 8 _gp. 1015-23 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1016/s0969-2126(03)00154-0 _zAvailable from publisher's website |
999 |
_c12681464 _d12681464 |