eF-site ID 6h12-AB PDB Code 6h12 Chain A, B click to enlarge Title Crystal structure of TcACHE complexed to 1-(6-Oxo-1,2,3,4,6,10b-hexahydropyrido[2,1-a]isoindol-10-yl)-3-(4-(((1-(2-((1,2,3,4-tetrahydroacridin-9-yl)amino)ethyl)-1H-1,2,3-triazol-4-yl)methoxy)methyl)pyridin-2-yl)urea Classification HYDROLASE Compound Acetylcholinesterase Source ORGANISM_COMMON: Pacific electric ray; ORGANISM_SCIENTIFIC: Tetronarce californica; Sequence A:  SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN EPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVF WNQFLPKLLNAT B:  SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN EPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVF WNQFLPKLLNAT Description Functional site 1) chain A residue 187-202 type prosite sequence FGGDPKTVTIFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG source prosite : PS00122 2) chain A residue 92-102 type prosite sequence EDCLYLNIWVP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP source prosite : PS00941 3) chain A residue 200 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 4) chain B residue 200 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 5) chain A residue 327 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 6) chain A residue 440 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 7) chain B residue 327 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 8) chain B residue 440 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 9) chain A residue 59 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558 source Swiss-Prot : SWS_FT_FI4 10) chain B residue 59 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 416 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899 source Swiss-Prot : SWS_FT_FI5 12) chain B residue 416 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899 source Swiss-Prot : SWS_FT_FI5 13) chain A residue 457 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI6 14) chain A residue 533 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI6 15) chain B residue 457 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI6 16) chain B residue 533 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI6

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