Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T30082 | Target Info | |||
| Target Name | Acetylcholinesterase (AChE) | ||||
| Synonyms | YT; N-ACHE; ARACHE | ||||
| Target Type | Successful Target | ||||
| Gene Name | ACHE | ||||
| Biochemical Class | Carboxylic ester hydrolase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Ethyl Dihydrogen Phosphate | Ligand Info | |||
| Canonical SMILES | CCOP(=O)(O)O | ||||
| InChI | 1S/C2H7O4P/c1-2-6-7(3,4)5/h2H2,1H3,(H2,3,4,5) | ||||
| InChIKey | ZJXZSIYSNXKHEA-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 74190 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5HF6 Crystal structure of human acetylcholinesterase in complex with paraoxon in the aged state | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [1] |
| PDB Sequence |
DAELLVTVRG
14 GRLRGIRLKT24 PGGPVSAFLG34 IPFAEPPMGP44 RRFLPPEPKQ54 PWSGVVDATT 64 FQSVCYQYVD74 TLYPGFEGTE84 MWNPNRELSE94 DCLYLNVWTP104 YPRPTSPTPV 114 LVWIYGGGFY124 SGASSLDVYD134 GRFLVQAERT144 VLVSMNYRVG154 AFGFLALPGS 164 REAPGNVGLL174 DQRLALQWVQ184 ENVAAFGGDP194 TSVTLFGESA204 GAASVGMHLL 214 SPPSRGLFHR224 AVLQSGAPNG234 PWATVGMGEA244 RRRATQLAHL254 VGCPNDTELV 270 ACLRTRPAQV280 LVNHEWHVLP290 QESVFRFSFV300 PVVDGDFLSD310 TPEALINAGD 320 FHGLQVLVGV330 VKDEGSYFLV340 YGAPGFSKDN350 ESLISRAEFL360 AGVRVGVPQV 370 SDLAAEAVVL380 HYTDWLHPED390 PARLREALSD400 VVGDHNVVCP410 VAQLAGRLAA 420 QGARVYAYVF430 EHRASTLSWP440 LWMGVPHGYE450 IEFIFGIPLD460 PSRNYTAEEK 470 IFAQRLMRYW480 ANFARTGDPN490 EPRAPQWPPY503 TAGAQQYVSL513 DLRPLEVRRG 523 LRAQACAFWN533 RFLPKLLS
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| PDB ID: 5HF8 Crystal structure of human acetylcholinesterase in complex with paraoxon (alternative acyl loop conformation) | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [1] |
| PDB Sequence |
EDAELLVTVR
13 GGRLRGIRLK23 TPGGPVSAFL33 GIPFAEPPMG43 PRRFLPPEPK53 QPWSGVVDAT 63 TFQSVCYQYV73 DTLYPGFEGT83 EMWNPNRELS93 EDCLYLNVWT103 PYPRPTSPTP 113 VLVWIYGGGF123 YSGASSLDVY133 DGRFLVQAER143 TVLVSMNYRV153 GAFGFLALPG 163 SREAPGNVGL173 LDQRLALQWV183 QENVAAFGGD193 PTSVTLFGES203 AGAASVGMHL 213 LSPPSRGLFH223 RAVLQSGAPN233 GPWATVGMGE243 ARRRATQLAH253 LVGCPNDTEL 269 VACLRTRPAQ279 VLVNHEWHVL289 PQESVFRFSF299 VPVVDGDFLS309 DTPEALINAG 319 DFHGLQVLVG329 VVKDEGSYFL339 VYGAPGFSKD349 NESLISRAEF359 LAGVRVGVPQ 369 VSDLAAEAVV379 LHYTDWLHPE389 DPARLREALS399 DVVGDHNVVC409 PVAQLAGRLA 419 AQGARVYAYV429 FEHRASTLSW439 PLWMGVPHGY449 EIEFIFGIPL459 DPSRNYTAEE 469 KIFAQRLMRY479 WANFARTGDP489 NEPRDPKAPQ499 WPPYTAGAQQ509 YVSLDLRPLE 519 VRRGLRAQAC529 AFWNRFLPKL539 LSA
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structures of paraoxon-inhibited human acetylcholinesterase reveal perturbations of the acyl loop and the dimer interface. Proteins. 2016 Sep;84(9):1246-56. | ||||
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