eF-site ID 2vjd-AB PDB Code 2vjd Chain A, B click to enlarge Title Torpedo Californica Acetylcholinesterase In Complex With A Non Hydrolysable Substrate Analogue, 4-Oxo-N,N,N- Trimethylpentanaminium - Orthorhombic space group - Dataset C at 150K Classification HYDROLASE Compound ACETYLCHOLINESTERASE Source ORGANISM_COMMON: PACIFIC ELECTRIC RAY; ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA; Sequence A:  SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN EPSKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQF LPKLLNAT 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 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_FI4 3) 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_FI4 4) chain A residue 457 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI5 5) chain A residue 533 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI5 6) chain B residue 457 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI5 7) chain B residue 533 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI5 8) 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_FI3 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_FI3 10) chain A residue 92-102 type prosite sequence EDCLYLNIWVP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP source prosite : PS00941 11) chain A residue 200 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 12) chain B residue 200 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 13) chain A residue 327 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 14) chain A residue 440 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 15) chain B residue 327 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 16) chain B residue 440 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2

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