eF-site ID 4da4-B PDB Code 4da4 Chain B click to enlarge Title Structure of mouse DNMT1 (731-1602) bound to hemimethylated CpG DNA Classification Transferase/DNA Compound DNA (cytosine-5)-methyltransferase 1 Source Mus musculus (Mouse) (4DA4) Sequence B:  DRISWLGQPMKIEENRTYYQKVSIDEEMLEVGDCVSVIPD DSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGAT SDPLELFLVGECENMQLSYIHSKVKVIYKAPSENWAMEGG GKTYFFQLWYNQEYARFESPPKTQPTEDNKHKFCLSCIRL AELRQKEMPKVLEQIEEVDGRVYCSSITKNGVVYRLGDSV YLPPEAFTFNIKVASPVKRPKKDPVNETLYPEHYRKYSDY IKGSNLDAPEPYRIGRIKEIHCGKKKGKVNEADIKLRLYK FYRPENTHRSYNGSYHTDINMLYWSDEEAVVNFSDVQGRC TVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPP NHARSPGNIKLPKLRTLDVFSGCGGLSEGFHQAGISETLW AIEMWDPAAQAFRLNNPGTTVFTEDCNVLLKLVMAGEVTN SLGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKN SLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLR CLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLP LFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTI TVRDTMSDLPEIQNGASNSEIPYNGEPLSWFQRQLRGSHY QPILRDHICKDMSPLVAARMRHIPLFPGSDWRDLPNIQVR LGDGVIAHKLQYTFHDVKNGYSSTGALRGVCSCAEGKACD PESRQFSTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTT VTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDSYRFF GNILDRHRQVGNAVPPPLAKAIGLEIKLCLLS Description Functional site 1) chain B residue 1148 type sequence F description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 2) chain B residue 1149 type sequence S description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 3) chain B residue 1150 type sequence G description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 4) chain B residue 1152 type sequence G description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 5) chain B residue 1153 type sequence G description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 6) chain B residue 1154 type sequence L description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 7) chain B residue 1171 type sequence E description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 8) chain B residue 1172 type sequence M description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 9) chain B residue 1173 type sequence W description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 10) chain B residue 1193 type sequence D description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 11) chain B residue 1194 type sequence C description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 12) chain B residue 1226 type sequence G description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 13) chain B residue 1247 type sequence K description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 14) chain B residue 1250 type sequence L description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 15) chain B residue 1581 type sequence A description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 16) chain B residue 1582 type sequence V description BINDING SITE FOR RESIDUE SAH B 1701 source : AC4 17) chain B residue 1479 type sequence C description BINDING SITE FOR RESIDUE ZN B 1702 source : AC5 18) chain B residue 1481 type sequence C description BINDING SITE FOR RESIDUE ZN B 1702 source : AC5 19) chain B residue 1487 type sequence C description BINDING SITE FOR RESIDUE ZN B 1702 source : AC5 20) chain B residue 1504 type sequence H description BINDING SITE FOR RESIDUE ZN B 1702 source : AC5 21) chain B residue 796 type sequence H description BINDING SITE FOR RESIDUE ZN B 1703 source : AC6 22) chain B residue 823 type sequence C description BINDING SITE FOR RESIDUE ZN B 1703 source : AC6 23) chain B residue 897 type sequence C description BINDING SITE FOR RESIDUE ZN B 1703 source : AC6 24) chain B residue 900 type sequence C description BINDING SITE FOR RESIDUE ZN B 1703 source : AC6 25) chain B residue 1566 type sequence R description BINDING SITE FOR RESIDUE CIT B 1704 source : AC7 26) chain B residue 1567 type sequence F description BINDING SITE FOR RESIDUE CIT B 1704 source : AC7 27) chain B residue 1568 type sequence F description BINDING SITE FOR RESIDUE CIT B 1704 source : AC7 28) chain B residue 1569 type sequence G description BINDING SITE FOR RESIDUE CIT B 1704 source : AC7 29) chain B residue 1574 type sequence R description BINDING SITE FOR RESIDUE CIT B 1704 source : AC7 30) chain B residue 1229 type ACT_SITE sequence C description ACT_SITE => ECO:0000269|PubMed:17576694 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 1149 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:4DA4 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 1153 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 1171 type BINDING sequence E description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 1582 type BINDING sequence V description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 1193 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 735 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 882 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 752 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6 39) chain B residue 895 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6 40) chain B residue 961 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6 41) chain B residue 965 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6 42) chain B residue 979 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6 43) chain B residue 1352 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6 44) chain B residue 1418 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P26358 source Swiss-Prot : SWS_FT_FI6

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