Research workbench
14-3-3 zeta bound to the phosphorylated 18E6 C-terminus
Analyse 14-3-3 zeta bound to the phosphorylated 18E6 C-terminus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZFD
- Type
- protein
- Length
- 481 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA,PROTEIN E6
- UniProt
- P63104, P06463
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA,PROTEIN E6 | protein | 241 | 79% helix, 0% strand | P63104, P06463 |
| B | 14-3-3 protein ZETA/DELTA,PROTEIN E6 | protein | 240 | 81% helix, 0% strand | P63104, P06463 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.53 | 0.76 | 25 | empty |
| 2 | 297 | 0.52 | 0.74 | 27 | empty |
| 3 | 197 | 0.51 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 954 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 P63104
- Every structure of UniProt P06463
- Elsewhere: RCSB PDB 6ZFD · PDBe 6ZFD · UniProt P63104 · UniProt P06463
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.