Crystal structure of hnRNP L RRM2 in complex with SETD2. Determined by X-ray diffraction at 1.8 Å resolution. Released 20 Oct 2021.
Explore 7EVR in 3D Show helices and sheets RCSB PDB PDBe
7EVR contains 5 α-helices and 20 β-strands across 4 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 | 194-200 | 7 | 1 |
| α-helix | 208-215 | 8 | |
| β-strand | 221-227 | 7 | 1 |
| β-strand | 232-238 | 7 | 1 |
| α-helix | 241-251 | 11 | |
| β-strand | 255-257 | 3 | 1 |
| β-strand | 260-267 | 8 | 1 |
| β-strand | 282-284 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2174-2175 | 2 | 1 |
| β-strand | 2179 | 1 | 2 |
| β-strand | 2182 | 1 | 2 |
| β-strand | 2187-2188 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 194-200 | 7 | 3 |
| α-helix | 208-215 | 8 | |
| α-helix | 216-218 | 3 | |
| β-strand | 221-227 | 7 | 3 |
| β-strand | 233-238 | 6 | 3 |
| α-helix | 241-251 | 11 | |
| β-strand | 255-257 | 3 | 3 |
| β-strand | 260-267 | 8 | 3 |
| β-strand | 282-284 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2174 | 1 | 3 |
| β-strand | 2179 | 1 | 4 |
| β-strand | 2182 | 1 | 4 |
| β-strand | 2188 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heterogeneous nuclear ribonucleoprotein L | A, C | protein | 111 | Homo sapiens | P14866 (AlphaFold model) |
| SHI domain from Histone-lysine N-methyltransferase SETD2 | B, D | protein | 26 | Homo sapiens | Q9BYW2 (AlphaFold model) |
>7EVR_1 Heterogeneous nuclear ribonucleoprotein L (chains A, C) HHHHHHMDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEF DSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPN
>7EVR_2 SHI domain from Histone-lysine N-methyltransferase SETD2 (chains B, D) YPPGYPMQAYVDPSNPNAGKVLLPTP
Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing. Bhattacharya, S., Wang, S., Reddy, D. et al. Nat Commun (2021) 12:6452-6452. DOI 10.1038/s41467-021-26799-3 · PubMed
Other PDB entries of the same protein (UniProt P14866 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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