eF-site ID 4ft2-ABP PDB Code 4ft2 Chain A, B, P click to enlarge Title crystal structure of Zea mays ZMET2 in complex H3(1-15)K9me2 peptide and SAH Classification TRANSFERASE Compound DNA (cytosine-5)-methyltransferase 1 Source Zea mays (Maize) (H31_HUMAN) Sequence A:  DHEPEFIGSPVAADEARSNWPKRYGLKARCHYRSAKVDNV VYCLGDDVYVKAGENEADYIGRITEFFEGTDQCHYFTCRW FFRAEDTVINSLVSISVDGHKHDPRRVFLSEEKNDNVLDC IISKVKIVHVDPNMDPKAKAQLIESCDLYYDMSYSVAYST FANISTRTATLLDLYSGCGGMSTGLCLGAALSGLKLETRW AVDFNSFACQSLKYNHPQTEVRNEKADEFLALLKEWAVLC KKYVVVEKLVGICYGGSDRENGIYFKVQWEGYGPEEDTWE PIDNLSDCPQKIREFVQEGHKRKILPLPGDVDVICGGPPC QKDEKNKQMVTFMDIVAYLKPKYVLMENVVDILKFADGYL GKYALSCLVAMKYQARLGMMVAGCYGLPQFRMRVFLWGAL SSMVLPKYPLPTYDVVVRGGAPNAFSQCMVAYDETQKPSL KKALLLGDAISDLPKVQNHQPNDVMEYGGSPKTEFQRYIR LSRKDMLDWSFGEGAGPDEGKLLDHQPLRLNNDDYERVQQ IPVKKGANFRDLKGVRVGANNIVEWDPEIERVKLSSGKPL VPDYAMSFIKGKSLKPFGRLWWDETVPTVVTRAEPHNQVI IHPTQARVLTIRENARLQGFPDYYRLFGPIKEKYIQVGNA VAVPVARALGYCLGQAYLGESEGSDPLYQLPPSF B:  EPEFIGSPVAADEARSNWPKRYLKARCHYRSAKVDNVVYC LGDDVYVKAGENEADYIGRITEFFEGTDQCHYFTCRWFFR AEDTVINSLVSISVDGHKHDPRRVFLSEEKNDNVLDCIIS KVKIVHVDPNMDPKAKAQLIESCDLYYDMSYSVAYSTFAN TRTATLLDLYSGCGGMSTGLCLGAALSGLKLETRWAVDFN SFACQSLKYNHPQTEVRNEKADEFLALLKEWAVLCKKYVE FVVEKLVGICYGGSDRENGIYFKVQWEGYGPEEDTWEPID NLSDCPQKIREFVQEGHKRKILPLPGDVDVICGGPPCQKD EKNKQMVTFMDIVAYLKPKYVLMENVVDILKFADGYLGKY ALSCLVAMKYQARLGMMVAGCYGLPQFRMRVFLWGALSSM VLPKYPLPTYDVVVRGGAPNAFSQCMVAYDETQKPSLKKA LLLGDAISDLPKVQNHQPNDVMEYGGSPKTEFQRYIRLSR KDMLDWSFGEGAGPDEGKLLDHQPLRLNNDDYERVQQIPV KKGANFRDLKGVRVGANNIVEWDPEIERVKLSSGKPLVPD YAMSFIKGKSLKPFGRLWWDETVPTVVTRAEPHNQVIIHP TQARVLTIRENARLQGFPDYYRLFGPIKEKYIQVGNAVAV PVARALGYCLGQAYLGESEGSDPLYQLPPS P:  QTARXST Description Functional site 1) chain A residue 347 type sequence Y description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 2) chain A residue 348 type sequence S description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 3) chain A residue 351 type sequence G description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 4) chain A residue 352 type sequence G description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 5) chain A residue 375 type sequence D description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 6) chain A residue 376 type sequence F description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 7) chain A residue 377 type sequence N description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 8) chain A residue 396 type sequence E description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 9) chain A residue 397 type sequence K description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 10) chain A residue 398 type sequence A description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 11) chain A residue 516 type sequence P description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 12) chain A residue 540 type sequence Q description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 13) chain A residue 852 type sequence A description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 14) chain A residue 853 type sequence V description BINDING SITE FOR RESIDUE SAH A 1000 source : AC1 15) chain B residue 347 type sequence Y description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 16) chain B residue 349 type sequence G description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 17) chain B residue 350 type sequence C description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 18) chain B residue 352 type sequence G description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 19) chain B residue 353 type sequence M description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 20) chain B residue 375 type sequence D description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 21) chain B residue 376 type sequence F description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 22) chain B residue 377 type sequence N description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 23) chain B residue 396 type sequence E description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 24) chain B residue 397 type sequence K description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 25) chain B residue 398 type sequence A description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 26) chain B residue 516 type sequence P description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 27) chain B residue 540 type sequence Q description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 28) chain B residue 559 type sequence E description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 29) chain B residue 851 type sequence N description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 30) chain B residue 852 type sequence A description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 31) chain B residue 853 type sequence V description BINDING SITE FOR RESIDUE SAH B 1000 source : AC2 32) chain P residue 9 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 517 type MOD_RES sequence C description Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1

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