eF-site ID 1kuv-A PDB Code 1kuv Chain A click to enlarge Title X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition Classification TRANSFERASE Compound Serotonin N-acetyltransferase Source (SNAT_SHEEP) Sequence A:  HTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNLDE VQHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESL ALHRPRGHSAHLHALAVHRSFRQQGKGSVLLWRYLHHVGA QPAVRRAVLMCEDALVPFYQRFGFHPAGPCAIVVGSLTFT EMHCSL Description Functional site 1) chain A residue 56 type sequence F description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 2) chain A residue 60 type sequence S description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 3) chain A residue 62 type sequence N description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 4) chain A residue 63 type sequence C description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 5) chain A residue 64 type sequence P description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 6) chain A residue 122 type sequence H description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 7) chain A residue 123 type sequence A description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 8) chain A residue 124 type sequence L description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 9) chain A residue 125 type sequence A description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 10) chain A residue 126 type sequence V description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 11) chain A residue 131 type sequence R description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 12) chain A residue 132 type sequence Q description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 13) chain A residue 132 type sequence Q description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 14) chain A residue 133 type sequence Q description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 15) chain A residue 134 type sequence G description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 16) chain A residue 136 type sequence G description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 17) chain A residue 137 type sequence S description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 18) chain A residue 154 type sequence R description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 19) chain A residue 159 type sequence M description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 20) chain A residue 160 type sequence C description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 21) chain A residue 161 type sequence E description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 22) chain A residue 164 type sequence L description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 23) chain A residue 167 type sequence F description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 24) chain A residue 168 type sequence Y description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 25) chain A residue 170 type sequence R description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 26) chain A residue 183 type sequence V description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 27) chain A residue 188 type sequence F description BINDING SITE FOR RESIDUE CA5 A 901 source : AC1 28) chain A residue 97 type catalytic sequence S description 22 source MCSA : MCSA1 29) chain A residue 111 type catalytic sequence L description 22 source MCSA : MCSA1 30) chain A residue 122 type catalytic sequence H description 22 source MCSA : MCSA1 31) chain A residue 124 type catalytic sequence L description 22 source MCSA : MCSA1 32) chain A residue 168 type catalytic sequence Y description 22 source MCSA : MCSA1 33) chain A residue 132 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11902838 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 168 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11902838 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 120 type SITE sequence H description Important for the catalytic mechanism; involved in substrate deprotonation => ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11884405 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 122 type SITE sequence H description Important for the catalytic mechanism; involved in substrate deprotonation => ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11884405 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 31 type MOD_RES sequence T description Phosphothreonine; by PKA => ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15644438 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 124 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11884405, ECO:0000269|PubMed:11902838 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 159 type BINDING sequence M description BINDING => ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11884405, ECO:0000269|PubMed:11902838 source Swiss-Prot : SWS_FT_FI1

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