MolNFT v1 · #138334 · protein
Structural basis for the interaction of 14-3-3BETA with tricarboxylic acid cycle intermediate malate
5WFU · 14-3-3 protein BETA/ALPHA: “Structural basis for the interaction of 14-3-3BETA with tricarboxylic acid cycle intermediate malate”. X-ray diffraction, 1 ligand (MLT), 9 pockets (best druggability 0.63). MolNFT v1 #138334 on…
- PDB
- 5WFU
- Type
- protein
- Length
- 934 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein BETA/ALPHA
- UniProt
- Q9CQV8
- Ligands
- MLT
- Pockets
- 9 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | 14-3-3 protein BETA/ALPHA | protein | 234 | 79% helix, 0% strand | Q9CQV8 |
| B, C | 14-3-3 protein BETA/ALPHA | protein | 233 | 79% helix, 0% strand | Q9CQV8 |
Ligands and binding sites
- MLT · D-malate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.63 | 0.77 | 50 | empty |
| 2 | 161 | 0.58 | 0.82 | 33 | empty |
| 3 | 308 | 0.55 | 0.76 | 24 | empty |
| 4 | 177 | 0.47 | 0.76 | 20 | empty |
| 5 | 179 | 0.45 | 0.75 | 25 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1198 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 612 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 606 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 174 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5WFU · Structural basis for the interaction of 14-3-3beta with Tricarboxylic Acid Cycle… · the same entry in another collection · chain D against D, TM-score 1.00
- Q9CQV8 · AlphaFold monomer V2.0 prediction for 14-3-3 protein BETA/ALPHA (Q9CQV8) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 Q9CQV8
- Elsewhere: RCSB PDB 5WFU · PDBe 5WFU · UniProt Q9CQV8
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