eF-site ID 1h3i-AB PDB Code 1h3i Chain A, B click to enlarge Title Crystal structure of the Histone Methyltransferase SET7/9 Classification TRANSFERASE Compound HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE Source Homo sapiens (Human) (Q8WTS6) Sequence A:  FFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGEL NGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGSLVG EVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLAT LMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPY ESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRIT HQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASL GHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEEL TVAYGYDHSPPGK B:  FFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGEL NGPAQEYDTDGRLIFKGQYKDNIRHGVCWIYYPDGGSLVG EVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLAT LMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPY ESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRIT HQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASL GHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEEL TVAYGYDHSPPGK Description (1)  HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE (E.C.2.1.1.43) Functional site 1) chain A residue 279 type sequence E description BINDING SITE FOR RESIDUE MG A1346 source : AC2 2) chain A residue 283 type sequence H description BINDING SITE FOR RESIDUE MG A1346 source : AC2 3) chain B residue 279 type sequence E description BINDING SITE FOR RESIDUE MG A1346 source : AC2 4) chain B residue 283 type sequence H description BINDING SITE FOR RESIDUE MG A1346 source : AC2 5) chain A residue 191 type catalytic sequence Y description 350 source MCSA : MCSA1 6) chain A residue 239 type catalytic sequence N description 350 source MCSA : MCSA1 7) chain A residue 243 type catalytic sequence S description 350 source MCSA : MCSA1 8) chain A residue 251 type catalytic sequence T description 350 source MCSA : MCSA1 9) chain A residue 281 type catalytic sequence Y description 350 source MCSA : MCSA1 10) chain B residue 191 type catalytic sequence Y description 350 source MCSA : MCSA2 11) chain B residue 239 type catalytic sequence N description 350 source MCSA : MCSA2 12) chain B residue 243 type catalytic sequence S description 350 source MCSA : MCSA2 13) chain B residue 251 type catalytic sequence T description 350 source MCSA : MCSA2 14) chain B residue 281 type catalytic sequence Y description 350 source MCSA : MCSA2 15) chain A residue 302 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 302 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 191 type SITE sequence Y description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 281 type SITE sequence Y description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 202 type SITE sequence S description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 212 type SITE sequence E description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 263 type SITE sequence N description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 281 type SITE sequence Y description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 191 type SITE sequence Y description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 202 type SITE sequence S description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 212 type SITE sequence E description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 263 type SITE sequence N description Histone H3K4 binding => ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 172 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 242 type BINDING sequence M description BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 243 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 172 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 242 type BINDING sequence M description BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 243 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 source Swiss-Prot : SWS_FT_FI1

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