Research workbench
Crystal structure of 14-3-3 epsilon with MLF1 peptide
Analyse Crystal structure of 14-3-3 epsilon with MLF1 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UAL
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein epsilon; Myeloid leukemia factor 1
- UniProt
- P62258, P58340
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein epsilon | protein | 230 | 85% helix, 0% strand | P62258 |
| P | Myeloid leukemia factor 1 | protein | 8 | 0% helix, 0% strand | P58340 |
Ligands and binding sites
- TBU · Tertiary-butyl alcohol · additive · 3 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.57 | 0.79 | 26 | empty |
| 2 | 81 | 0.54 | 0.85 | 13 | TBU |
| 3 | 56 | 0.30 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–P · 641 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3UAL · Crystal Structure of 14-3-3 epsilon with Mlf1 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P62258 · AlphaFold monomer V2.0 prediction for 14-3-3 protein epsilon (P62258) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P58340 · AlphaFold monomer V2.0 prediction for myeloid leukemia factor 1 (P58340) · a predicted model of the same protein · chain P against A, TM-score 0.34
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 P62258
- Every structure of UniProt P58340
- Elsewhere: RCSB PDB 3UAL · PDBe 3UAL · UniProt P62258 · UniProt P58340
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