Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T99799 | Target Info | |||
| Target Name | Cholinesterase (BCHE) | ||||
| Synonyms | Pseudocholinesterase; Choline esterase II; CHE1; Butyrylcholine esterase; Acylcholine acylhydrolase | ||||
| Target Type | Successful Target | ||||
| Gene Name | BCHE | ||||
| Biochemical Class | Type-B carboxylesterase/lipase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | alpha-L-Fucose | Ligand Info | |||
| Canonical SMILES | CC1C(C(C(C(O1)O)O)O)O | ||||
| InChI | 1S/C6H12O5/c1-2-3(7)4(8)5(9)6(10)11-2/h2-10H,1H3/t2-,3+,4+,5-,6+/m0/s1 | ||||
| InChIKey | SHZGCJCMOBCMKK-SXUWKVJYSA-N | ||||
| PubChem Compound ID | 439554 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4XII X-ray structure of human butyrylcholinesterase in complex with N-((1-(2,3-dihydro-1H-inden-2-yl)piperidin-3-yl)methyl)-8-hydroxy-N-(2-methoxyethyl)-5-nitroquinoline-7-carboxamide | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [1] |
| PDB Sequence |
DIIIATKNGK
12 VRGMNLTVFG22 GTVTAFLGIP32 YAQPPLGRLR42 FKKPQSLTKW52 SDIWNATKYA 62 NSCCQNIDQS72 FPGFHGSEMW82 NPNTDLSEDC92 LYLNVWIPAP102 KPKNATVLIW 112 IYGGGFQTGT122 SSLHVYDGKF132 LARVERVIVV142 SMNYRVGALG152 FLALPGNPEA 162 PGNMGLFDQQ172 LALQWVQKNI182 AAFGGNPKSV192 TLFGESAGAA202 SVSLHLLSPG 212 SHSLFTRAIL222 QSGSFNAPWA232 VTSLYEARNR242 TLNLAKLTGC252 SRENETEIIK 262 CLRNKDPQEI272 LLNEAFVVPY282 GTPLSVNFGP292 TVDGDFLTDM302 PDILLELGQF 312 KKTQILVGVN322 KDEGTAFLVY332 GAPGFSKDNN342 SIITRKEFQE352 GLKIFFPGVS 362 EFGKESILFH372 YTDWVDDQRP382 ENYREALGDV392 VGDYNFICPA402 LEFTKKFSEW 412 GNNAFFYYFE422 HRSSKLPWPE432 WMGVMHGYEI442 EFVFGLPLER452 RDNYTKAEEI 462 LSRSIVKRWA472 NFAKYGNPNE482 TQNNSTSWPV492 FKSTEQKYLT502 LNTESTRIMT 512 KLRAQQCRFW522 TSFFPKVL
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| PDB ID: 4BDS Human butyrylcholinesterase in complex with tacrine | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [2] |
| PDB Sequence |
IIIATKNGKV
13 RGMQLTVFGG23 TVTAFLGIPY33 AQPPLGRLRF43 KKPQSLTKWS53 DIWNATKYAN 63 SCCQNIDQSF73 PGFHGSEMWN83 PNTDLSEDCL93 YLNVWIPAPK103 PKNATVLIWI 113 YGGGFQTGTS123 SLHVYDGKFL133 ARVERVIVVS143 MNYRVGALGF153 LALPGNPEAP 163 GNMGLFDQQL173 ALQWVQKNIA183 AFGGNPKSVT193 LFGESAGAAS203 VSLHLLSPGS 213 HSLFTRAILQ223 SGSFNAPWAV233 TSLYEARNRT243 LNLAKLTGCS253 RENETEIIKC 263 LRNKDPQEIL273 LNEAFVVPYG283 TPLSVNFGPT293 VDGDFLTDMP303 DILLELGQFK 313 KTQILVGVNK323 DEGTAFLVYG333 APGFSKDNNS343 IITRKEFQEG353 LKIFFPGVSE 363 FGKESILFHY373 TDWVQRPENY385 REALGDVVGD395 YNFICPALEF405 TKKFSEWGNN 415 AFFYYFEHRS425 SKLPWPEWMG435 VMHGYEIEFV445 FGLPLERRDQ455 YTKAEEILSR 465 SIVKRWANFA475 KYGNPQETQN485 QSTSWPVFKS495 TEQKYLTLNT505 ESTRIMTKLR 515 AQQCRFWTSF525 FPKV
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| PDB ID: 2Y1K STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP (12H SOAK): PHOSPHOSERINE ADDUCT | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | Yes | [3] |
| PDB Sequence |
DIIIATKNGK
12 VRGMQLTVFG22 GTVTAFLGIP32 YAQPPLGRLR42 FKKPQSLTKW52 SDIWNATKYA 62 NSCCQNIDQS72 FPGFHGSEMW82 NPNTDLSEDC92 LYLNVWIPAP102 KPKNATVLIW 112 IYGGGFQTGT122 SSLHVYDGKF132 LARVERVIVV142 SMNYRVGALG152 FLALPGNPEA 162 PGNMGLFDQQ172 LALQWVQKNI182 AAFGGNPKSV192 TLFGEAGAAS203 VSLHLLSPGS 213 HSLFTRAILQ223 SGSFNAPWAV233 TSLYEARNRT243 LNLAKLTGCS253 RENETEIIKC 263 LRNKDPQEIL273 LNEAFVVPYG283 TPLSVNFGPT293 VDGDFLTDMP303 DILLELGQFK 313 KTQILVGVNK323 DEGTAFLVYG333 APGFSKDNNS343 IITRKEFQEG353 LKIFFPGVSE 363 FGKESILFHY373 TDWVDDRPEN384 YREALGDVVG394 DYNFICPALE404 FTKKFSEWGN 414 NAFFYYFEHR424 SSKLPWPEWM434 GVMHGYEIEF444 VFGLPLERRD454 QYTKAEEILS 464 RSIVKRWANF474 AKYGNPQETQ484 NNSTSWPVFK494 STEQKYLTLN504 TESTRIMTKL 514 RAQQCRFWTS524 FFPKV
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| PDB ID: 2XQK X-ray Structure of human butyrylcholinesterase inhibited by pure enantiomer VX-(S) | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | Yes | [4] |
| PDB Sequence |
DIIIATKNGK
12 VRGMQLTVFG22 GTVTAFLGIP32 YAQPPLGRLR42 FKKPQSLTKW52 SDIWNATKYA 62 NSCCQNIDQS72 FPGFHGSEMW82 NPNTDLSEDC92 LYLNVWIPAP102 KPKNATVLIW 112 IYGGGFQTGT122 SSLHVYDGKF132 LARVERVIVV142 SMNYRVGALG152 FLALPGNPEA 162 PGNMGLFDQQ172 LALQWVQKNI182 AAFGGNPKSV192 TLFGESAGAA202 SVSLHLLSPG 212 SHSLFTRAIL222 QSGSFNAPWA232 VTSLYEARNR242 TLNLAKLTGC252 SRENETEIIK 262 CLRNKDPQEI272 LLNEAFVVPY282 GTPLSVNFGP292 TVDGDFLTDM302 PDILLELGQF 312 KKTQILVGVN322 KDEGTAFLVY332 GAPGFSKDNN342 SIITRKEFQE352 GLKIFFPGVS 362 EFGKESILFH372 YTDWVDDQRP382 ENYREALGDV392 VGDYNFICPA402 LEFTKKFSEW 412 GNNAFFYYFE422 HRSSKLPWPE432 WMGVMHGYEI442 EFVFGLPLER452 RDQYTKAEEI 462 LSRSIVKRWA472 NFAKYGNPQE482 TQNQSTSWPV492 FKSTEQKYLT502 LNTESTRIMT 512 KLRAQQCRFW522 TSFFPKV
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Click to Show 3D Structure of This Binding Site
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure-based development of nitroxoline derivatives as potential multifunctional anti-Alzheimer agents. Bioorg Med Chem. 2015 Aug 1;23(15):4442-4452. | ||||
| REF 2 | Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase. Biochem J. 2013 Aug 1;453(3):393-9. | ||||
| REF 3 | Reaction of cresyl saligenin phosphate, the organophosphorus agent implicated in aerotoxic syndrome, with human cholinesterases: mechanistic studies employing kinetics, mass spectrometry, and X-ray structure analysis. Chem Res Toxicol. 2011 Jun 20;24(6):797-808. | ||||
| REF 4 | Structural study of the complex stereoselectivity of human butyrylcholinesterase for the neurotoxic V-agents. J Biol Chem. 2011 May 13;286(19):16783-9. | ||||
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