Research workbench
Crystal structure of hnRNP L RRM2 in complex with SETD2
Analyse Crystal structure of hnRNP L 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
- 7EVR
- Type
- protein
- Length
- 251 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Heterogeneous nuclear ribonucleoprotein L; SHI domain from Histone-lysine…
- EC
- 2.1.1.359, 2.1.1.-
- UniProt
- P14866, Q9BYW2
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · resolution 1.8 · 3 distinct chains · 18% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heterogeneous nuclear ribonucleoprotein L | protein | 100 | 19% helix, 35% strand | P14866 |
| B, D | SHI domain from Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.359, 2.1.1.-) | protein | 26 | 0% helix, 23% strand | Q9BYW2 |
| C | Heterogeneous nuclear ribonucleoprotein L | protein | 99 | 22% helix, 34% strand | P14866 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.38 | 0.76 | 23 | empty |
| 2 | 91 | 0.34 | 0.74 | 26 | empty |
Interfaces
4 interfaces between chains.
- C–D · 555 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 541 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 253 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 188 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7EVR · Crystal structure of hnrnp L RRM2 in complex with SETD2 · the same entry in another collection · chain A against A, TM-score 1.00
- P14866 · AlphaFold monomer V2.0 prediction for heterogeneous nuclear ribonucleoprotein L (P14866) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q9BYW2 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD2 (Q9BYW2) · a predicted model of the same protein · chain B against A, TM-score 0.24
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 P14866
- Every structure of UniProt Q9BYW2
- Elsewhere: RCSB PDB 7EVR · PDBe 7EVR · UniProt P14866 · UniProt Q9BYW2
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