Research workbench
Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by 14-3-3
Analyse Molecular basis for the recognition of phosphorylated and phosphoacetylated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C1N
- Type
- protein
- Length
- 466 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein ZETA/DELTA; Histone H3 acetylphosphopeptide
- UniProt
- P63104
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 14-3-3 protein ZETA/DELTA | protein | 225 | 79% helix, 0% strand | P63104 |
| C, E | Histone H3 acetylphosphopeptide | protein | 8 | 0% helix, 0% strand | — |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.58 | 0.79 | 34 | empty |
| 2 | 266 | 0.58 | 0.78 | 32 | empty |
| 3 | 351 | 0.54 | 0.74 | 27 | empty |
| 4 | 53 | 0.28 | 0.74 | 14 | empty |
| 5 | 60 | 0.27 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 936 Ų buried · 10 hydrogen bonds · protein-protein
- B–E · 509 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 494 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 2C1N · Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by… · the same entry in another collection · chain A against A, TM-score 1.00
- P63104 · AlphaFold monomer V2.0 prediction for 14-3-3 protein ZETA/DELTA (P63104) · a predicted model of the same protein · chain A against A, TM-score 0.99
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
- Elsewhere: RCSB PDB 2C1N · PDBe 2C1N · UniProt P63104
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.