eF-site ID 1yah-ABC PDB Code 1yah Chain A, B, C click to enlarge Title Crystal Structure of Human Liver Carboxylesterase complexed to Etyl Acetate; A Fatty Acid Ethyl Ester Analogue Classification HYDROLASE Compound CES1 protein Source (EST1_HUMAN) Sequence A:  SSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSEL FTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIH GGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGE SAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD VKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERN FHTVPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSL LWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLI ADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKP KTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWA NFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKD KEVAFWTNLFAK B:  SSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSEL FTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIH GGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGE SAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD VKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERN FHTVPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSL LWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLI ADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKP KTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWA NFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKD KEVAFWTNLFAK C:  SSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSEL FTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIH GGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGE SAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD VKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERN FHTVPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSL LWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLI ADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKP KTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWA NFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKD KEVAFWTNLFAK Description Functional site 1) chain A residue 221 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 221 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 221 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 354 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 469 type ACT_SITE sequence G description Charge relay system => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 354 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI2 7) chain B residue 469 type ACT_SITE sequence G description Charge relay system => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI2 8) chain C residue 354 type ACT_SITE sequence E description Charge relay system => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI2 9) chain C residue 469 type ACT_SITE sequence G description Charge relay system => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 381 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 11) chain B residue 381 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 12) chain C residue 381 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 79 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 79 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI4 15) chain C residue 79 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12022871 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 208-223 type prosite sequence FGGNPGSVTIFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpgsVtIfGeSAG source prosite : PS00122 17) chain A residue 114-124 type prosite sequence EDCLYLNIYTP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIYtP source prosite : PS00941

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