Crystal structure of the chromodomain-ATPase portion of the yeast Chd1 chromatin remodeler. Determined by X-ray diffraction at 3.7 Å resolution. Released 29 Sept 2010.
Explore 3MWY in 3D Show helices and sheets RCSB PDB PDBe
3MWY contains 39 α-helices and 28 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 | 178 | 1 | 1 |
| β-strand | 181-186 | 6 | 2 |
| α-helix | 204-210 | 7 | |
| β-strand | 212-216 | 5 | 2 |
| α-helix | 217 | 1 | |
| β-strand | 226-228 | 3 | 2 |
| α-helix | 230-233 | 4 | |
| β-strand | 237 | 1 | 1 |
| α-helix | 240-246 | 7 | |
| α-helix | 247-251 | 5 | |
| α-helix | 252-256 | 5 | |
| α-helix | 264-281 | 18 | |
| β-strand | 287-290 | 4 | 3 |
| α-helix | 295 | 1 | |
| β-strand | 296-297 | 2 | 4 |
| β-strand | 303-304 | 2 | 4 |
| β-strand | 306 | 1 | 5 |
| β-strand | 309-311 | 3 | 3 |
| β-strand | 320 | 1 | 3 |
| β-strand | 323 | 1 | 5 |
| α-helix | 324-327 | 4 | |
| α-helix | 332-340 | 9 | |
| α-helix | 379-391 | 13 | |
| β-strand | 397-399 | 3 | 6 |
| α-helix | 401-402 | 2 | |
| α-helix | 409-422 | 14 | |
| β-strand | 428-431 | 4 | 7 |
| α-helix | 437-447 | 11 | |
| β-strand | 453-455 | 3 | 7 |
| α-helix | 461-470 | 10 | |
| β-strand | 487-490 | 4 | 7 |
| α-helix | 494-497 | 4 | |
| α-helix | 499-503 | 5 | |
| β-strand | 506-512 | 7 | 7 |
| α-helix | 515-518 | 4 | |
| α-helix | 524-529 | 6 | |
| β-strand | 533-537 | 5 | 7 |
| β-strand | 538-540 | 3 | 6 |
| α-helix | 550-559 | 10 | |
| α-helix | 578-588 | 11 | |
| α-helix | 591-593 | 3 | |
| β-strand | 594-596 | 3 | 6 |
| α-helix | 599-602 | 4 | |
| β-strand | 609-616 | 8 | 8 |
| α-helix | 617-619 | 3 | |
| α-helix | 620-632 | 13 | |
| α-helix | 648-660 | 13 | |
| α-helix | 662-664 | 3 | |
| α-helix | 668-672 | 5 | |
| α-helix | 684-692 | 9 | |
| α-helix | 695-707 | 13 | |
| β-strand | 714-718 | 5 | 8 |
| α-helix | 721-734 | 14 | |
| β-strand | 739-741 | 3 | 8 |
| α-helix | 747-755 | 9 | |
| β-strand | 767-770 | 4 | 8 |
| α-helix | 771-774 | 4 | |
| β-strand | 785-788 | 4 | 8 |
| α-helix | 796-802 | 7 | |
| β-strand | 814-821 | 8 | 8 |
| α-helix | 825-836 | 12 | |
| α-helix | 862-869 | 8 | |
| α-helix | 880-887 | 8 | |
| α-helix | 891-897 | 7 | |
| β-strand | 899-900 | 2 | 8 |
| β-strand | 911-912 | 2 | 6 |
| α-helix | 915-919 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chromo domain-containing protein 1 | W | protein | 800 | Saccharomyces cerevisiae | P32657 (AlphaFold model) |
>3MWY_1 Chromo domain-containing protein 1 (chains W) GPSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEK TVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLD PYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEA TWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDF QLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPA WLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDR AELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFL MPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELS DVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDG KMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQ RLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADL QAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNE PNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLK QFEVTDYKADIDWDDIIPEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 1 |
The chromodomains of the Chd1 chromatin remodeler regulate DNA access to the ATPase motor. Hauk, G., McKnight, J.N., Nodelman, I.M. et al. Mol Cell (2010) 39:711-723. DOI 10.1016/j.molcel.2010.08.012 · PubMed
Other PDB entries of the same protein (UniProt P32657 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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