eF-site ID 5jiy-B PDB Code 5jiy Chain B 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 B:  EKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCE TSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDK DGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKV RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEAD VREDDSYLFDLDEVYCIDARYYGNISRFINHLCDPNIIPV RVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIK SKYFTCQCGSEKCKHSAEAIALEQSRL Description Functional site 1) chain B residue 974 type sequence C description binding site for residue ZN B 1201 source : AC6 2) chain B residue 987 type sequence C description binding site for residue ZN B 1201 source : AC6 3) chain B residue 1017 type sequence C description binding site for residue ZN B 1201 source : AC6 4) chain B residue 1021 type sequence C description binding site for residue ZN B 1201 source : AC6 5) chain B residue 980 type sequence C description binding site for residue ZN B 1202 source : AC7 6) chain B residue 1017 type sequence C description binding site for residue ZN B 1202 source : AC7 7) chain B residue 1023 type sequence C description binding site for residue ZN B 1202 source : AC7 8) chain B residue 1027 type sequence C description binding site for residue ZN B 1202 source : AC7 9) chain B residue 974 type sequence C description binding site for residue ZN B 1203 source : AC8 10) chain B residue 976 type sequence C description binding site for residue ZN B 1203 source : AC8 11) chain B residue 980 type sequence C description binding site for residue ZN B 1203 source : AC8 12) chain B residue 985 type sequence C description binding site for residue ZN B 1203 source : AC8 13) chain B residue 1115 type sequence C description binding site for residue ZN B 1204 source : AC9 14) chain B residue 1168 type sequence C description binding site for residue ZN B 1204 source : AC9 15) chain B residue 1170 type sequence C description binding site for residue ZN B 1204 source : AC9 16) chain B residue 1175 type sequence C description binding site for residue ZN B 1204 source : AC9 17) chain B residue 1048 type sequence M description binding site for residue SAM B 1205 source : AD1 18) chain B residue 1050 type sequence W description binding site for residue SAM B 1205 source : AD1 19) chain B residue 1084 type sequence S description binding site for residue SAM B 1205 source : AD1 20) chain B residue 1085 type sequence Y description binding site for residue SAM B 1205 source : AD1 21) chain B residue 1109 type sequence R description binding site for residue SAM B 1205 source : AD1 22) chain B residue 1110 type sequence F description binding site for residue SAM B 1205 source : AD1 23) chain B residue 1112 type sequence N description binding site for residue SAM B 1205 source : AD1 24) chain B residue 1113 type sequence H description binding site for residue SAM B 1205 source : AD1 25) chain B residue 1154 type sequence Y description binding site for residue SAM B 1205 source : AD1 26) chain B residue 1166 type sequence F description binding site for residue SAM B 1205 source : AD1 27) chain B residue 1167 type sequence T description binding site for residue SAM B 1205 source : AD1 28) chain B residue 1168 type sequence C description binding site for residue SAM B 1205 source : AD1 29) chain B residue 1169 type sequence Q description binding site for residue SAM B 1205 source : AD1 30) chain B residue 1008 type MOD_RES sequence K description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 1010 type MOD_RES sequence E description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI1 32) chain B 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 33) chain B 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 34) chain B 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 35) chain B 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 36) chain B 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 B 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 B 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 B 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 40) chain B 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 41) chain B 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 42) chain B 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

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