Crystal structure of MLL1 PHD3-Bromo in the free form. Determined by X-ray diffraction at 1.72 Å resolution. Released 7 Jul 2010.
Explore 3LQH in 3D Show helices and sheets RCSB PDB PDBe
3LQH contains 9 α-helices and 4 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 | 1568 | 1 | 1 |
| β-strand | 1575 | 1 | 1 |
| β-strand | 1585-1587 | 3 | 2 |
| β-strand | 1594-1596 | 3 | 2 |
| α-helix | 1597-1599 | 3 | |
| α-helix | 1604-1612 | 9 | |
| α-helix | 1614-1617 | 4 | |
| α-helix | 1631-1652 | 22 | |
| α-helix | 1655-1661 | 7 | |
| α-helix | 1708-1716 | 9 | |
| α-helix | 1723-1740 | 18 | |
| α-helix | 1745-1765 | 21 | |
| α-helix | 1771-1773 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-lysine N-methyltransferase MLL | A | protein | 183 | Homo sapiens | Q03164 |
>3LQH_1 Histone-lysine N-methyltransferase MLL (chains A) SGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNC TERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQQQPLDLEGVKRKMDQGNYT SVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNK VSS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Wang, Z., Song, J., Milne, T.A. et al. Cell (2010) 141:1183-1194. DOI 10.1016/j.cell.2010.05.016 · PubMed
Other PDB entries of the same protein (UniProt Q03164), best resolution first:
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