Research workbench
Crystal structure of hnRNP LL RRM2 in complex with SETD2
Analyse Crystal structure of hnRNP LL RRM2 in complex with SETD2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EVS
- Type
- protein
- Length
- 227 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Heterogeneous nuclear ribonucleoprotein L-like; SHI domain from Histone-lysine…
- UniProt
- Q8WVV9, Q9BYW2
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · resolution 1.6 · 3 distinct chains · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Heterogeneous nuclear ribonucleoprotein L-like | protein | 101 | 19% helix, 36% strand | Q8WVV9 |
| C | SHI domain from Histone-lysine N-methyltransferase SETD2 | protein | 12 | 0% helix, 8% strand | Q9BYW2 |
| D | SHI domain from Histone-lysine N-methyltransferase SETD2 | protein | 13 | 0% helix, 8% strand | Q9BYW2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.57 | 0.77 | 24 | empty |
| 2 | 89 | 0.52 | 0.83 | 20 | empty |
| 3 | 93 | 0.50 | 0.82 | 16 | empty |
| 4 | 99 | 0.42 | 0.78 | 25 | empty |
Interfaces
5 interfaces between chains.
- B–D · 513 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 508 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 354 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 217 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 209 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7EVS · Crystal structure of hnrnp ll RRM2 in complex with SETD2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8WVV9 · AlphaFold monomer V2.0 prediction for heterogeneous nuclear ribonucleoprotein L-like… · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q9BYW2 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD2 (Q9BYW2) · a predicted model of the same protein · chain C against A, TM-score 0.34
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8WVV9
- Every structure of UniProt Q9BYW2
- Elsewhere: RCSB PDB 7EVS · PDBe 7EVS · UniProt Q8WVV9 · UniProt Q9BYW2
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