000 | 01467 a2200373 4500 | ||
---|---|---|---|
005 | 20250514015753.0 | ||
264 | 0 | _c20020123 | |
008 | 200201s 0 0 eng d | ||
022 | _a0907-4449 | ||
024 | 7 |
_a10.1107/s090744490101575x _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aSousa, M C | |
245 | 0 | 0 |
_aStructure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. _h[electronic resource] |
260 |
_bActa crystallographica. Section D, Biological crystallography _cDec 2001 |
||
300 |
_a1950-4 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 | _aATP-Dependent Proteases |
650 | 0 | 4 |
_aAdenosine Triphosphatases _xchemistry |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aCatalysis |
650 | 0 | 4 |
_aCations _xmetabolism |
650 | 0 | 4 | _aCrystallization |
650 | 0 | 4 | _aCrystallography, X-Ray |
650 | 0 | 4 |
_aEndopeptidases _xchemistry |
650 | 0 | 4 |
_aHaemophilus influenzae _xchemistry |
650 | 0 | 4 | _aHeat-Shock Proteins |
650 | 0 | 4 | _aHydrolysis |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aSerine Endopeptidases |
700 | 1 | _aMcKay, D B | |
773 | 0 |
_tActa crystallographica. Section D, Biological crystallography _gvol. 57 _gno. Pt 12 _gp. 1950-4 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1107/s090744490101575x _zAvailable from publisher's website |
999 |
_c11632023 _d11632023 |