Research workbench
Crystal structure of FUS3 with a docking motif from STE7
Analyse Crystal structure of FUS3 with a docking motif from STE7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B9H
- Type
- protein
- Length
- 349 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase FUS3; SERINE/THREONINE-protein kinase STE7
- EC
- 2.7.1.37
- UniProt
- P16892
- Ligands
- ADP, MG
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase FUS3 (EC 2.7.1.37) | protein | 337 | 40% helix, 14% strand | P16892 |
| C | SERINE/THREONINE-protein kinase STE7 (EC 2.7.1.37) | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 268 | 0.62 | 0.80 | 34 | MG, ADP |
| 2 | 53 | 0.47 | 0.85 | 13 | empty |
| 3 | 88 | 0.37 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–C · 674 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2B9H · Crystal structure of Fus3 with a docking motif from Ste7 · the same entry in another collection · chain A against A, TM-score 1.00
- P16892 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase FUS3 (P16892) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P16892
- Elsewhere: RCSB PDB 2B9H · PDBe 2B9H · UniProt P16892
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