Research workbench
14-3-3 ZETA/PHOSPHOPEPTIDE complex (mode 1)
Analyse 14-3-3 ZETA/PHOSPHOPEPTIDE complex (mode 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QJB
- Type
- protein
- Length
- 475 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Phosphopeptide
- UniProt
- P29312
- Pockets
- 6 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein ZETA/DELTA | protein | 228 | 77% helix, 0% strand | P29312 |
| B | 14-3-3 protein ZETA/DELTA | protein | 232 | 80% helix, 0% strand | P29312 |
| Q | Phosphopeptide | protein | 8 | 0% helix, 0% strand | — |
| S | Phosphopeptide | protein | 7 | 0% helix, 0% strand | — |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.54 | 0.81 | 25 | empty |
| 2 | 322 | 0.53 | 0.75 | 27 | empty |
| 3 | 83 | 0.48 | 0.82 | 19 | empty |
| 4 | 121 | 0.44 | 0.77 | 24 | empty |
| 5 | 78 | 0.37 | 0.77 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1059 Ų buried · 11 hydrogen bonds · protein-protein
- A–Q · 617 Ų buried · 16 hydrogen bonds · protein-protein
- B–S · 566 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 1QJB · 14-3-3 ZETA/PHOSPHOPEPTIDE complex (mode 1) · 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 P29312
- Elsewhere: RCSB PDB 1QJB · PDBe 1QJB · UniProt P29312
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.