EC Number   |
|---|
   3.4.23.46 | 6 x His-tagged proBACE1 |
| 3.4.23.46 | BACE-1 in complex with inhibitor N-[(1S,2S,4R)-4-((S)-1-benzylcarbamoyl-2-methylpropylcarbamoyl)-1-(3,5-difluoro-phenoxymethyl)-2-hydroxy-4-(2-methoxy-ethoxy)-butyl]-5-(methanesulfonyl-methylamino)-N'-((R)-1-phenyl-ethyl)-isophthalamide |
| 3.4.23.46 | conformational study of BACE1 inhibitor shown, molecular surface model and stereoview indicated |
| 3.4.23.46 | conformational study of BACE1 inhibitor, molecular surface model and stereoview indicated |
| 3.4.23.46 | evolutionary trace analysis identifies group-specific residues in the ligand binding sites of BACE1, and BACE2, EC 3.4.23.45.The residues are Pro70, Ile110, Ile126, andAsn233 of BACE1 substituting Lys86, Leu126, Leu142, and Leu246 of BACE2, respectively.These group-specific residues would be the reason for cleavage site selectivity in BACE1 and BACE2 biological function |
| 3.4.23.46 | hanging drop vapor diffusion method, using 6% (w/v) PEG3350, 0.1 M sodium acetate, pH 5.4 |
| 3.4.23.46 | in complex with inhibitor (2R,4S)-N-butyl-4-[(2S,5S,7R)-2,7-dimethyl-3,15-dioxo-1,4-diazacyclopentadecan-5-yl]-4-hydroxy-2-methylbutanamide |
| 3.4.23.46 | in complex with inhibitor (2S)-2-((3R)-3-acetamido-3-isobutyl-2-oxo-1-pyrrolidinyl)-N-((1S,2R)-1-(3,5-difluorobenzyl)-2-hydroxy-2-(1,2,3,4-tetrahydro-3-isoquinolinyl)ethyl)-4-phenylbutanamide |
| 3.4.23.46 | in complex with inhibitor (3S,14R,16S)-16-[(1R)-1-hydroxy-2-([3-(1-methylethyl)benzyl]amino)ethyl]-3,4,14-trimethyl-1,4-diazacyclohexadecane-2,5-dione. The lipophilic isopropylbenzyl moiety of inhibitor is bound into the P2' subsite, lined on one side by the flap residues Val69, Pro70, Tyr71 and Thr72 and, on the other side, by Tyr198. In addition to hydrophobic contacts to Ser35, Val69, Tyr71 and Tyr198, this P' group is rather rigid, the position and orientation of the benzyl ring is not optimal for strong pi-stacking interactions with either Tyr71 or Tyr198 |
| 3.4.23.46 | in complex with inhibitor (S)-7-(2-fluoropyridin-3-yl)-3-((3-methyloxetan-3-yl)ethynyl)-5H-spiro[chromeno[2,3-b]pyridine-5,4-oxazol]-2-amine. The aminooxazoline unit engages in hydrogen-bonding interactions with the catalytic aspartic acid residues of the enzyme, and the nitrogen atom of the 2-pyridyl-3-fluoro group interacts with Ser229 via a bridging water molecule in the S3 pocket |
