Structure of the replication foci-targeting sequence of human DNA cytosine methyltransferase DNMT1. Determined by X-ray diffraction at 2.31 Å resolution. Released 25 Nov 2008.
Explore 3EPZ in 3D Show helices and sheets RCSB PDB PDBe
3EPZ contains 26 α-helices and 33 β-strands across 2 chains. 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 | 352 | 1 | 1 |
| β-strand | 359 | 1 | 1 |
| β-strand | 367 | 1 | 2 |
| β-strand | 375 | 1 | 3 |
| α-helix | 377-389 | 13 | |
| β-strand | 405-409 | 5 | 3 |
| β-strand | 410 | 1 | 4 |
| β-strand | 411-413 | 3 | 3 |
| β-strand | 418 | 1 | 2 |
| β-strand | 419 | 1 | 3 |
| β-strand | 434-441 | 8 | 3 |
| β-strand | 453-458 | 6 | 3 |
| β-strand | 463-467 | 5 | 3 |
| β-strand | 474 | 1 | 5 |
| β-strand | 476-480 | 5 | 3 |
| β-strand | 485-488 | 4 | 3 |
| α-helix | 490 | 1 | |
| β-strand | 491 | 1 | 4 |
| α-helix | 492 | 1 | |
| α-helix | 496-499 | 4 | |
| α-helix | 504-518 | 15 | |
| α-helix | 524-533 | 10 | |
| α-helix | 534 | 1 | |
| β-strand | 535 | 1 | 5 |
| α-helix | 536-537 | 2 | |
| α-helix | 538-540 | 3 | |
| α-helix | 543-545 | 3 | |
| α-helix | 547-551 | 5 | |
| α-helix | 554-567 | 14 | |
| α-helix | 575-577 | 3 | |
| α-helix | 579-587 | 9 | |
| α-helix | 592-598 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 352 | 1 | 6 |
| β-strand | 359 | 1 | 6 |
| β-strand | 367 | 1 | 7 |
| β-strand | 375 | 1 | 8 |
| α-helix | 377-381 | 5 | |
| β-strand | 404-407 | 4 | 9 |
| β-strand | 408-409 | 2 | 8 |
| β-strand | 410 | 1 | 10 |
| β-strand | 411-413 | 3 | 8 |
| β-strand | 418 | 1 | 7 |
| β-strand | 419 | 1 | 8 |
| β-strand | 434-439 | 6 | 8 |
| α-helix | 440-441 | 2 | |
| β-strand | 453-455 | 3 | 8 |
| β-strand | 463-466 | 4 | 9 |
| β-strand | 477-480 | 4 | 9 |
| β-strand | 485-488 | 4 | 9 |
| β-strand | 491 | 1 | 10 |
| α-helix | 496-499 | 4 | |
| α-helix | 504-519 | 16 | |
| α-helix | 524-533 | 10 | |
| α-helix | 538-540 | 3 | |
| α-helix | 542-545 | 4 | |
| α-helix | 547-551 | 5 | |
| α-helix | 554-566 | 13 | |
| α-helix | 579-588 | 10 | |
| α-helix | 594-596 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA (cytosine-5)-methyltransferase 1 | A, B | protein | 268 | Homo sapiens | P26358 (AlphaFold model) |
>3EPZ_1 DNA (cytosine-5)-methyltransferase 1 (chains A, B) MHHHHHHSSGRENLYFQGPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDAN ESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGG VNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIV VEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDE QPIFLTPCMRDLIKLAGVTLGQRRAQAR
Water and common crystallization additives (NA, GOL) are not listed.
The replication focus targeting sequence (RFTS) domain is a DNA-competitive inhibitor of Dnmt1. Syeda, F., Fagan, R.L., Wean, M. et al. J Biol Chem (2011) 286:15344-15351. DOI 10.1074/jbc.M110.209882 · 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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