eF-site ID 5jiy-A PDB Code 5jiy Chain A 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 null (5JIY) Sequence A:  IRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISE NCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCW YDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSG IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDA EADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLC DPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG DRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSR 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 A residue 1082 type MOD_RES sequence D description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 1119 type MOD_RES sequence I description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 1146 type MOD_RES sequence T description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 1149 type MOD_RES sequence E description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 1055 type MOD_RES sequence L description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 1057 type MOD_RES sequence T description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 1061 type MOD_RES sequence G description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 1014 type MOD_RES sequence I description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 1019 type MOD_RES sequence Q description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 1021 type MOD_RES sequence C description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 1051 type MOD_RES sequence G description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1

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