Human DNMT1(729-1600) Bound to Zebularine-Containing 12mer dsDNA and Cofactor SAM. Determined by X-ray diffraction at 2.43 Å resolution. Released 30 Mar 2022.
Explore 7SFG in 3D Show helices and sheets RCSB PDB PDBe
7SFG contains 50 α-helices and 55 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 |
|---|---|---|---|
| β-strand | 731-734 | 4 | 1 |
| β-strand | 740 | 1 | 2 |
| β-strand | 744-747 | 4 | 2 |
| β-strand | 749-752 | 4 | 1 |
| β-strand | 755-758 | 4 | 1 |
| β-strand | 762-765 | 4 | 2 |
| α-helix | 773-774 | 2 | |
| β-strand | 775-785 | 11 | 2 |
| β-strand | 790-799 | 10 | 2 |
| α-helix | 800-802 | 3 | |
| α-helix | 806-808 | 3 | |
| β-strand | 813-824 | 12 | 2 |
| α-helix | 825-827 | 3 | |
| β-strand | 828-832 | 5 | 2 |
| β-strand | 834-836 | 3 | 2 |
| α-helix | 838-840 | 3 | |
| α-helix | 843-845 | 3 | |
| β-strand | 863-870 | 8 | 2 |
| β-strand | 875-877 | 3 | 2 |
| α-helix | 878-880 | 3 | |
| α-helix | 894-906 | 13 | |
| β-strand | 909-910 | 2 | 3 |
| β-strand | 913-916 | 4 | 4 |
| β-strand | 920-923 | 4 | 4 |
| β-strand | 925-928 | 4 | 3 |
| β-strand | 931-934 | 4 | 3 |
| β-strand | 938-941 | 4 | 4 |
| α-helix | 970-975 | 6 | |
| α-helix | 987-991 | 5 | |
| β-strand | 992-1002 | 11 | 4 |
| β-strand | 1003 | 1 | 5 |
| α-helix | 1004 | 1 | |
| β-strand | 1009 | 1 | 5 |
| β-strand | 1015-1020 | 6 | 4 |
| α-helix | 1021 | 1 | |
| β-strand | 1022 | 1 | 6 |
| α-helix | 1023 | 1 | |
| α-helix | 1024-1026 | 3 | |
| α-helix | 1033-1036 | 4 | |
| β-strand | 1041-1044 | 4 | 7 |
| β-strand | 1048-1052 | 5 | 4 |
| α-helix | 1053-1055 | 3 | |
| β-strand | 1058-1060 | 3 | 4 |
| β-strand | 1061-1064 | 4 | 7 |
| α-helix | 1072-1077 | 6 | |
| β-strand | 1082-1088 | 7 | 7 |
| β-strand | 1090 | 1 | 8 |
| β-strand | 1095 | 1 | 8 |
| α-helix | 1098-1100 | 3 | |
| α-helix | 1101-1103 | 3 | |
| α-helix | 1137-1138 | 2 | |
| β-strand | 1139-1144 | 6 | 2 |
| α-helix | 1150-1157 | 8 | |
| β-strand | 1161-1167 | 7 | 2 |
| α-helix | 1171-1180 | 10 | |
| β-strand | 1185-1187 | 3 | 2 |
| α-helix | 1191-1199 | 9 | |
| β-strand | 1204 | 1 | 9 |
| α-helix | 1209 | 1 | |
| β-strand | 1210 | 1 | 9 |
| α-helix | 1211-1212 | 2 | |
| β-strand | 1219-1222 | 4 | 2 |
| α-helix | 1243-1245 | 3 | |
| α-helix | 1247-1258 | 12 | |
| β-strand | 1262-1268 | 7 | 2 |
| α-helix | 1269-1272 | 4 | |
| α-helix | 1274-1290 | 17 | |
| β-strand | 1293-1300 | 8 | 2 |
| α-helix | 1301-1304 | 4 | |
| β-strand | 1308 | 1 | 10 |
| β-strand | 1311-1318 | 8 | 2 |
| α-helix | 1323-1330 | 8 | |
| β-strand | 1332 | 1 | 11 |
| α-helix | 1336-1339 | 4 | |
| β-strand | 1343-1345 | 3 | 12 |
| β-strand | 1348-1350 | 3 | 12 |
| β-strand | 1362 | 1 | 11 |
| α-helix | 1363-1365 | 3 | |
| α-helix | 1367-1371 | 5 | |
| α-helix | 1375-1376 | 2 | |
| β-strand | 1385-1386 | 2 | 13 |
| α-helix | 1395-1401 | 7 | |
| β-strand | 1409-1410 | 2 | 13 |
| α-helix | 1419-1426 | 8 | |
| α-helix | 1436-1438 | 3 | |
| β-strand | 1444-1445 | 2 | 14 |
| β-strand | 1451-1452 | 2 | 14 |
| β-strand | 1453 | 1 | 15 |
| α-helix | 1454-1455 | 2 | |
| β-strand | 1494 | 1 | 15 |
| α-helix | 1499-1503 | 5 | |
| α-helix | 1504-1506 | 3 | |
| α-helix | 1508-1510 | 3 | |
| α-helix | 1515 | 1 | |
| β-strand | 1516 | 1 | 16 |
| α-helix | 1517 | 1 | |
| β-strand | 1523 | 1 | 10 |
| α-helix | 1524-1525 | 2 | |
| β-strand | 1540 | 1 | 16 |
| β-strand | 1547 | 1 | 16 |
| α-helix | 1548-1549 | 2 | |
| α-helix | 1550-1556 | 7 | |
| α-helix | 1569-1577 | 9 | |
| α-helix | 1580-1581 | 2 | |
| α-helix | 1582-1599 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA (cytosine-5)-methyltransferase 1 | A | protein | 874 | Homo sapiens | P26358 (AlphaFold model) |
| DNA Strand 1 | C | DNA | 12 | Homo sapiens | |
| DNA Strand 2 | D | DNA | 12 | Homo sapiens |
>7SFG_1 DNA (cytosine-5)-methyltransferase 1 (chains A) HMNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDS SNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAME GGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKE IPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDE DLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPEN THKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFL EAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFS GCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNS RGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLE NVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPL FPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEI SYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRL SDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNR HNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLF GNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKA
>7SFG_2 DNA Strand 1 (chains C) GAGGCCGCCTGC
>7SFG_3 DNA Strand 2 (chains D) GCAGGUGGCCTC
Water and common crystallization additives (EDO, GOL) are not listed.
Structural characterization of dicyanopyridine containing DNMT1-selective, non-nucleoside inhibitors. Horton, J.R., Pathuri, S., Wong, K. et al. Structure (2022) 30:793-802.e5. DOI 10.1016/j.str.2022.03.009 · PubMed
Other PDB entries of the same protein (UniProt P26358 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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