Research workbench
Complex of chrebp and 14-3-3BETA
Analyse Complex of chrebp and 14-3-3BETA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GNT
- Type
- protein
- Length
- 252 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein BETA/ALPHA; Carbohydrate-responsive element-binding protein
- UniProt
- Q9CQV8, Q99MZ3
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein BETA/ALPHA | protein | 231 | 83% helix, 0% strand | Q9CQV8 |
| B | Carbohydrate-responsive element-binding protein | protein | 21 | 81% helix, 0% strand | Q99MZ3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 549 | 0.67 | 0.77 | 38 | SO4 |
| 2 | 107 | 0.43 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 872 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4GNT · Complex of ChREBP and 14-3-3beta · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.98
- Q99MZ3 · AlphaFold monomer V2.0 prediction for carbohydrate-responsive element-binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.56
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
- Every structure of UniProt Q99MZ3
- Elsewhere: RCSB PDB 4GNT · PDBe 4GNT · UniProt Q9CQV8 · UniProt Q99MZ3
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