Crystal Structure of the Bromodomain of human ASH1L. Determined by X-ray diffraction at 2.54 Å resolution. Released 19 May 2010.
Explore 3MQM in 3D Show helices and sheets RCSB PDB PDBe
3MQM contains 16 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 2433-2453 | 21 | |
| β-strand | 2455 | 1 | 1 |
| β-strand | 2461 | 1 | 1 |
| α-helix | 2464-2466 | 3 | |
| α-helix | 2469-2471 | 3 | |
| α-helix | 2472-2474 | 3 | |
| α-helix | 2478-2481 | 4 | |
| α-helix | 2488-2497 | 10 | |
| α-helix | 2503-2521 | 19 | |
| α-helix | 2526-2553 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2433-2453 | 21 | |
| β-strand | 2455-2456 | 2 | 2 |
| β-strand | 2460-2461 | 2 | 2 |
| α-helix | 2464-2466 | 3 | |
| α-helix | 2469-2471 | 3 | |
| α-helix | 2472-2474 | 3 | |
| α-helix | 2478-2481 | 4 | |
| α-helix | 2488-2497 | 10 | |
| α-helix | 2503-2521 | 19 | |
| α-helix | 2526-2553 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Probable histone-lysine N-methyltransferase ASH1L | A, B | protein | 126 | Homo sapiens | Q9NR48 |
>3MQM_1 Probable histone-lysine N-methyltransferase ASH1L (chains A, B) SMEVARAARLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLIT IEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLRKAYYNARHEASAQID EIVGET
Histone recognition and large-scale structural analysis of the human bromodomain family. Filippakopoulos, P., Picaud, S., Mangos, M. et al. Cell (2012) 149:214-231. DOI 10.1016/j.cell.2012.02.013 · PubMed
Other PDB entries of the same protein (UniProt Q9NR48), best resolution first:
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