Research workbench
Crystal structure of 14-3-3 epsilon with FOXO3A peptide
Analyse Crystal structure of 14-3-3 epsilon with FOXO3A peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V9B
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- YWHAE/FAM22B fusion protein; Arg-arg-arg-ala-val-sep-met-asp-asn-ser-asn
- UniProt
- G9K389
- Ligands
- 323
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | YWHAE/FAM22B fusion protein | protein | 231 | 86% helix, 0% strand | G9K389 |
| B | Arg-arg-arg-ala-val-sep-met-asp-asn-ser-asn | protein | 8 | 0% helix, 0% strand | — |
Ligands and binding sites
- 323 · 2-[3,6-bis(dimethylamino)xanthen-9-yl]-5-methanoyl-benzoate · ligand · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
- IMD · Imidazole · additive · chains A
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 | 232 | 0.59 | 0.79 | 25 | empty |
| 2 | 74 | 0.46 | 0.82 | 14 | GOL |
| 3 | 109 | 0.43 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 533 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, phosphorylation).
Compared structures
- 7V9B · Crystal Structure of 14-3-3 epsilon with FOXO3a peptide · the same entry in another collection · chain A against A, TM-score 1.00
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 G9K389
- Elsewhere: RCSB PDB 7V9B · PDBe 7V9B · UniProt G9K389
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