Research workbench
Structure of 14-3-3 beta in complex with tfeb 14-3-3 binding motif
Analyse Structure of 14-3-3 beta in complex with tfeb 14-3-3 binding motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A5Q
- Type
- protein
- Length
- 727 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein BETA/ALPHA; Tfeb PS211-peptide
- UniProt
- P31946
- Pockets
- 6 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | 14-3-3 protein BETA/ALPHA | protein | 232 | 85% helix, 0% strand | P31946 |
| C | 14-3-3 protein BETA/ALPHA | protein | 226 | 85% helix, 0% strand | P31946 |
| D, F | Tfeb PS211-peptide | protein | 12 | 0% helix, 0% strand | — |
| E | Tfeb PS211-peptide | protein | 13 | 0% helix, 0% strand | — |
Ligands and binding sites
- MLA · Malonic acid · additive · 3 copies · chains B, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.55 | 0.75 | 26 | empty |
| 2 | 90 | 0.41 | 0.78 | 16 | empty |
| 3 | 69 | 0.40 | 0.80 | 13 | empty |
| 4 | 68 | 0.31 | 0.74 | 13 | empty |
| 5 | 68 | 0.29 | 0.73 | 17 | empty |
Interfaces
6 interfaces between chains.
- B–A · 1106 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 962 Ų buried · 24 hydrogen bonds · protein-protein
- A–F · 945 Ų buried · 26 hydrogen bonds · protein-protein
- B–E · 945 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 116 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 6A5Q · Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif · the same entry in another collection · chain F against F, TM-score 1.00
- P31946 · AlphaFold monomer V2.0 prediction for 14-3-3 protein BETA/ALPHA (P31946) · 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 P31946
- Elsewhere: RCSB PDB 6A5Q · PDBe 6A5Q · UniProt P31946
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