MolNFT v1 · #32464 · protein
14-3-3 protein epsilon (human) complexed to peptide
2BR9: “14-3-3 protein epsilon (human) complexed to peptide”. X-ray diffraction, 3 pockets (best druggability 0.54). MolNFT v1 #32464 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2BR9
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein epsilon; Consensus peptide for 14-3-3 proteins
- UniProt
- P62258
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein epsilon | protein | 230 | 86% helix, 0% strand | P62258 |
| P | Consensus peptide for 14-3-3 proteins | protein | 6 | 0% helix, 0% strand | — |
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 | 164 | 0.54 | 0.80 | 20 | empty |
| 2 | 64 | 0.41 | 0.80 | 14 | empty |
| 3 | 65 | 0.32 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–P · 508 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
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
- Elsewhere: RCSB PDB 2BR9 · PDBe 2BR9 · UniProt P62258
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.