MolNFT v1 · #118603 · protein
Crystal structure of CHREBP:14-3-3 complex bound with AMP
5F74 · 14-3-3 protein BETA/ALPHA: “Crystal structure of CHREBP:14-3-3 complex bound with AMP”. X-ray diffraction, 1 ligand (AMP), 2 pockets (best druggability 0.66). MolNFT v1 #118603 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5F74
- Type
- protein
- Length
- 249 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, Q8VIP2
- Ligands
- AMP
- Pockets
- 2 · best druggability 0.66
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 | 229 | 83% helix, 0% strand | Q9CQV8 |
| B | Carbohydrate-responsive element-binding protein | protein | 20 | 85% helix, 0% strand | Q8VIP2 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 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 | 532 | 0.66 | 0.77 | 37 | AMP |
| 2 | 94 | 0.45 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 873 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 5F74 · Crystal structure of ChREBP:14-3-3 complex bound with AMP · 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 0.99
- Q8VIP2 · AlphaFold monomer V2.0 prediction for carbohydrate-responsive element-binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.53
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 Q8VIP2
- Elsewhere: RCSB PDB 5F74 · PDBe 5F74 · UniProt Q9CQV8 · UniProt Q8VIP2
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