eF-site ID 5jiy-ABFG PDB Code 5jiy Chain A, B, F, G click to enlarge Title Structure of G9a SET-domain with Histone H3K9norLeucine mutant peptide and bound S-adenosylmethionine Classification TRANSFERASE Compound Histone-lysine N-methyltransferase EHMT2 Source Homo sapiens (Human) (5JIY) Sequence A:  IRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISE NCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCW YDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSG IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDA EADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLC DPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG DRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSR B:  EKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCE TSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDK DGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKV RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEAD VREDDSYLFDLDEVYCIDARYYGNISRFINHLCDPNIIPV RVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIK SKYFTCQCGSEKCKHSAEAIALEQSRL F:  KQTARXST G:  TKQTARXST Description Functional site 1) chain A residue 974 type sequence C description binding site for residue ZN A 1201 source : AC1 2) chain A residue 987 type sequence C description binding site for residue ZN A 1201 source : AC1 3) chain A residue 1017 type sequence C description binding site for residue ZN A 1201 source : AC1 4) chain A residue 1021 type sequence C description binding site for residue ZN A 1201 source : AC1 5) chain A residue 974 type sequence C description binding site for residue ZN A 1202 source : AC2 6) chain A residue 976 type sequence C description binding site for residue ZN A 1202 source : AC2 7) chain A residue 980 type sequence C description binding site for residue ZN A 1202 source : AC2 8) chain A residue 985 type sequence C description binding site for residue ZN A 1202 source : AC2 9) chain A residue 980 type sequence C description binding site for residue ZN A 1203 source : AC3 10) chain A residue 1017 type sequence C description binding site for residue ZN A 1203 source : AC3 11) chain A residue 1023 type sequence C description binding site for residue ZN A 1203 source : AC3 12) chain A residue 1027 type sequence C description binding site for residue ZN A 1203 source : AC3 13) chain A residue 1115 type sequence C description binding site for residue ZN A 1204 source : AC4 14) chain A residue 1168 type sequence C description binding site for residue ZN A 1204 source : AC4 15) chain A residue 1170 type sequence C description binding site for residue ZN A 1204 source : AC4 16) chain A residue 1175 type sequence C description binding site for residue ZN A 1204 source : AC4 17) chain A residue 1048 type sequence M description binding site for residue SAM A 1205 source : AC5 18) chain A residue 1050 type sequence W description binding site for residue SAM A 1205 source : AC5 19) chain A residue 1084 type sequence S description binding site for residue SAM A 1205 source : AC5 20) chain A residue 1085 type sequence Y description binding site for residue SAM A 1205 source : AC5 21) chain A residue 1109 type sequence R description binding site for residue SAM A 1205 source : AC5 22) chain A residue 1110 type sequence F description binding site for residue SAM A 1205 source : AC5 23) chain A residue 1111 type sequence I description binding site for residue SAM A 1205 source : AC5 24) chain A residue 1112 type sequence N description binding site for residue SAM A 1205 source : AC5 25) chain A residue 1113 type sequence H description binding site for residue SAM A 1205 source : AC5 26) chain A residue 1154 type sequence Y description binding site for residue SAM A 1205 source : AC5 27) chain A residue 1158 type sequence F description binding site for residue SAM A 1205 source : AC5 28) chain A residue 1166 type sequence F description binding site for residue SAM A 1205 source : AC5 29) chain A residue 1167 type sequence T description binding site for residue SAM A 1205 source : AC5 30) chain A residue 1168 type sequence C description binding site for residue SAM A 1205 source : AC5 31) chain A residue 1169 type sequence Q description binding site for residue SAM A 1205 source : AC5 32) chain F residue 9 type sequence X description binding site for residue SAM A 1205 source : AC5 33) chain B residue 974 type sequence C description binding site for residue ZN B 1201 source : AC6 34) chain B residue 987 type sequence C description binding site for residue ZN B 1201 source : AC6 35) chain B residue 1017 type sequence C description binding site for residue ZN B 1201 source : AC6 36) chain B residue 1021 type sequence C description binding site for residue ZN B 1201 source : AC6 37) chain B residue 980 type sequence C description binding site for residue ZN B 1202 source : AC7 38) chain B residue 1017 type sequence C description binding site for residue ZN B 1202 source : AC7 39) chain B residue 1023 type sequence C description binding site for residue ZN B 1202 source : AC7 40) chain B residue 1027 type sequence C description binding site for residue ZN B 1202 source : AC7 41) chain B residue 974 type sequence C description binding site for residue ZN B 1203 source : AC8 42) chain B residue 976 type sequence C description binding site for residue ZN B 1203 source : AC8 43) chain B residue 980 type sequence C description binding site for residue ZN B 1203 source : AC8 44) chain B residue 985 type sequence C description binding site for residue ZN B 1203 source : AC8 45) chain B residue 1115 type sequence C description binding site for residue ZN B 1204 source : AC9 46) chain B residue 1168 type sequence C description binding site for residue ZN B 1204 source : AC9 47) chain B residue 1170 type sequence C description binding site for residue ZN B 1204 source : AC9 48) chain B residue 1175 type sequence C description binding site for residue ZN B 1204 source : AC9 49) chain B residue 1048 type sequence M description binding site for residue SAM B 1205 source : AD1 50) chain B residue 1050 type sequence W description binding site for residue SAM B 1205 source : AD1 51) chain B residue 1084 type sequence S description binding site for residue SAM B 1205 source : AD1 52) chain B residue 1085 type sequence Y description binding site for residue SAM B 1205 source : AD1 53) chain B residue 1109 type sequence R description binding site for residue SAM B 1205 source : AD1 54) chain B residue 1110 type sequence F description binding site for residue SAM B 1205 source : AD1 55) chain B residue 1112 type sequence N description binding site for residue SAM B 1205 source : AD1 56) chain B residue 1113 type sequence H description binding site for residue SAM B 1205 source : AD1 57) chain B residue 1154 type sequence Y description binding site for residue SAM B 1205 source : AD1 58) chain B residue 1166 type sequence F description binding site for residue SAM B 1205 source : AD1 59) chain B residue 1167 type sequence T description binding site for residue SAM B 1205 source : AD1 60) chain B residue 1168 type sequence C description binding site for residue SAM B 1205 source : AD1 61) chain B residue 1169 type sequence Q description binding site for residue SAM B 1205 source : AD1 62) chain A residue 1082 type MOD_RES sequence D description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 63) chain A residue 1119 type MOD_RES sequence I description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 64) chain A residue 1146 type MOD_RES sequence T description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 1149 type MOD_RES sequence E description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 1008 type MOD_RES sequence K description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 67) chain B residue 1010 type MOD_RES sequence E description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 1014 type MOD_RES sequence I description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 1019 type MOD_RES sequence Q description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 1021 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 71) chain B residue 1051 type MOD_RES sequence G description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 72) chain G residue 3 type MOD_RES sequence T description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 73) chain B residue 1055 type MOD_RES sequence L description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 1057 type MOD_RES sequence T description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 1061 type MOD_RES sequence G description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 1082 type MOD_RES sequence D description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 77) chain B residue 1119 type MOD_RES sequence I description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 78) chain B residue 1146 type MOD_RES sequence T description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 79) chain B residue 1149 type MOD_RES sequence E description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 1014 type MOD_RES sequence I description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 81) chain A residue 1019 type MOD_RES sequence Q description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 82) chain A residue 1021 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 83) chain A residue 1051 type MOD_RES sequence G description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 84) chain A residue 1055 type MOD_RES sequence L description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 85) chain A residue 1057 type MOD_RES sequence T description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 86) chain A residue 1061 type MOD_RES sequence G description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI1 87) chain F residue 4 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 88) chain G residue 4 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 89) chain F residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI3 90) chain G residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI3 91) chain F residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI4 92) chain G residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI4 93) chain F residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI5 94) chain G residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI5 95) chain F residue 9 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI6 96) chain G residue 9 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI6 97) chain F residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI7 98) chain G residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI7 99) chain F residue 11 type MOD_RES sequence T description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 source Swiss-Prot : SWS_FT_FI8 100) chain G residue 11 type MOD_RES sequence T description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 source Swiss-Prot : SWS_FT_FI8

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