Structure of human DNMT1 (601-1600) in complex with Sinefungin. Determined by X-ray diffraction at 2.49 Å resolution. Released 10 Aug 2011.
Explore 3SWR in 3D Show helices and sheets RCSB PDB PDBe
3SWR contains 54 α-helices and 60 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 618-619 | 2 | |
| α-helix | 622-629 | 8 | |
| β-strand | 651 | 1 | 1 |
| α-helix | 670-672 | 3 | |
| α-helix | 687-689 | 3 | |
| β-strand | 695 | 1 | 1 |
| β-strand | 723 | 1 | 2 |
| α-helix | 724-726 | 3 | |
| β-strand | 731-734 | 4 | 3 |
| β-strand | 741 | 1 | 4 |
| β-strand | 744-746 | 3 | 4 |
| β-strand | 749-752 | 4 | 3 |
| β-strand | 755-758 | 4 | 3 |
| β-strand | 759 | 1 | 5 |
| β-strand | 761 | 1 | 5 |
| β-strand | 762-765 | 4 | 4 |
| β-strand | 767 | 1 | 2 |
| β-strand | 775-785 | 11 | 4 |
| β-strand | 789-799 | 11 | 4 |
| α-helix | 800-802 | 3 | |
| α-helix | 806-808 | 3 | |
| β-strand | 813-824 | 12 | 4 |
| α-helix | 825-827 | 3 | |
| β-strand | 828-832 | 5 | 4 |
| β-strand | 834-836 | 3 | 4 |
| α-helix | 843-845 | 3 | |
| α-helix | 856-860 | 5 | |
| β-strand | 863-870 | 8 | 4 |
| β-strand | 875-877 | 3 | 4 |
| α-helix | 878-880 | 3 | |
| α-helix | 894-905 | 12 | |
| β-strand | 909-910 | 2 | 6 |
| β-strand | 913-916 | 4 | 7 |
| β-strand | 921-923 | 3 | 7 |
| β-strand | 925-928 | 4 | 6 |
| β-strand | 931-934 | 4 | 6 |
| β-strand | 938-941 | 4 | 7 |
| α-helix | 973-975 | 3 | |
| α-helix | 976-980 | 5 | |
| α-helix | 983-987 | 5 | |
| β-strand | 992-1001 | 10 | 7 |
| α-helix | 1009-1010 | 2 | |
| β-strand | 1015-1020 | 6 | 7 |
| α-helix | 1021 | 1 | |
| β-strand | 1022 | 1 | 8 |
| α-helix | 1024-1026 | 3 | |
| α-helix | 1031-1034 | 4 | |
| β-strand | 1041-1044 | 4 | 9 |
| β-strand | 1048-1052 | 5 | 7 |
| α-helix | 1053-1055 | 3 | |
| β-strand | 1058-1060 | 3 | 7 |
| β-strand | 1061-1064 | 4 | 9 |
| α-helix | 1065-1067 | 3 | |
| α-helix | 1072-1077 | 6 | |
| β-strand | 1082-1090 | 9 | 9 |
| β-strand | 1095-1097 | 3 | 9 |
| α-helix | 1136-1138 | 3 | |
| β-strand | 1139-1144 | 6 | 4 |
| α-helix | 1150-1158 | 9 | |
| β-strand | 1161-1167 | 7 | 4 |
| α-helix | 1171-1180 | 10 | |
| β-strand | 1185-1187 | 3 | 4 |
| α-helix | 1191-1200 | 10 | |
| β-strand | 1204 | 1 | 10 |
| β-strand | 1210 | 1 | 10 |
| β-strand | 1219-1222 | 4 | 4 |
| α-helix | 1234-1235 | 2 | |
| α-helix | 1237-1243 | 7 | |
| α-helix | 1247-1258 | 12 | |
| β-strand | 1262-1268 | 7 | 4 |
| α-helix | 1269-1272 | 4 | |
| α-helix | 1275-1277 | 3 | |
| α-helix | 1278-1290 | 13 | |
| β-strand | 1293-1300 | 8 | 4 |
| α-helix | 1301-1304 | 4 | |
| β-strand | 1308 | 1 | 11 |
| β-strand | 1311-1318 | 8 | 4 |
| α-helix | 1327-1330 | 4 | |
| β-strand | 1332 | 1 | 12 |
| α-helix | 1336-1338 | 3 | |
| β-strand | 1343-1345 | 3 | 13 |
| β-strand | 1348-1350 | 3 | 13 |
| β-strand | 1362 | 1 | 12 |
| α-helix | 1363-1365 | 3 | |
| α-helix | 1367-1371 | 5 | |
| α-helix | 1375-1376 | 2 | |
| β-strand | 1385-1386 | 2 | 14 |
| α-helix | 1395-1401 | 7 | |
| β-strand | 1409-1410 | 2 | 14 |
| α-helix | 1419-1426 | 8 | |
| α-helix | 1436-1438 | 3 | |
| β-strand | 1444-1445 | 2 | 15 |
| β-strand | 1451-1452 | 2 | 15 |
| β-strand | 1453 | 1 | 16 |
| α-helix | 1454-1455 | 2 | |
| β-strand | 1459 | 1 | 17 |
| β-strand | 1474 | 1 | 17 |
| α-helix | 1477-1479 | 3 | |
| α-helix | 1487-1489 | 3 | |
| β-strand | 1494 | 1 | 16 |
| α-helix | 1499-1503 | 5 | |
| α-helix | 1504-1506 | 3 | |
| α-helix | 1508-1510 | 3 | |
| α-helix | 1515 | 1 | |
| β-strand | 1516 | 1 | 18 |
| α-helix | 1517 | 1 | |
| β-strand | 1523 | 1 | 11 |
| β-strand | 1540 | 1 | 18 |
| β-strand | 1547 | 1 | 18 |
| α-helix | 1548-1549 | 2 | |
| α-helix | 1550-1556 | 7 | |
| α-helix | 1569-1578 | 10 | |
| α-helix | 1580-1581 | 2 | |
| α-helix | 1582-1598 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA (cytosine-5)-methyltransferase 1 | A | protein | 1002 | Homo sapiens | P26358 (AlphaFold model) |
>3SWR_1 DNA (cytosine-5)-methyltransferase 1 (chains A) HMRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEV CQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKM HQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLAR VTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKA PSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCAR LAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKR PRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRV NKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMG GPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPK LRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLV MAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYY RPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAA APGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVR NGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRD LPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPW CLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQG FPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKA
Water and common crystallization additives (SO4, MES, EDO) are not listed.
Structure of human DNMT1 (residues 600-1600) in complex with Sinefungin. Hashimoto, H., Cheng, X. To be published.
Other PDB entries of the same protein (UniProt P26358 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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