Research workbench
CH1 chimera of human 14-3-3 sigma with the HSPB6 phosphopeptide in a conformation with self-bound phosphopeptides
Analyse CH1 chimera of human 14-3-3 sigma with the HSPB6 phosphopeptide in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OKF
- Type
- protein
- Length
- 920 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein SIGMA,HEAT shock protein beta-6
- UniProt
- P31947, O14558
- Ligands
- CD
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein SIGMA,HEAT shock protein beta-6 | protein | 231 | 81% helix, 0% strand | P31947, O14558 |
| B | 14-3-3 protein SIGMA,HEAT shock protein beta-6 | protein | 228 | 80% helix, 0% strand | P31947, O14558 |
| C | 14-3-3 protein SIGMA,HEAT shock protein beta-6 | protein | 231 | 79% helix, 0% strand | P31947, O14558 |
| D | 14-3-3 protein SIGMA,HEAT shock protein beta-6 | protein | 230 | 82% helix, 0% strand | P31947, O14558 |
Ligands and binding sites
- CD · Cadmium ion · metal · 17 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.76 | 0.83 | 81 | CD |
| 2 | 422 | 0.76 | 0.85 | 68 | CD |
| 3 | 276 | 0.58 | 0.78 | 22 | empty |
| 4 | 183 | 0.55 | 0.79 | 20 | empty |
| 5 | 328 | 0.55 | 0.75 | 24 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1028 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1015 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 586 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 552 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 14 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (oxidation, phosphorylation).
Compared structures
- 5OKF · CH1 chimera of human 14-3-3 sigma with the HSPB6 phosphopeptide in a conformation with… · the same entry in another collection · chain A against A, TM-score 1.00
- P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain A against A, TM-score 0.95
- O14558 · AlphaFold monomer V2.0 prediction for heat shock protein beta-6 (O14558) · a predicted model of the same protein · chain A against A, TM-score 0.22
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 P31947
- Every structure of UniProt O14558
- Elsewhere: RCSB PDB 5OKF · PDBe 5OKF · UniProt P31947 · UniProt O14558
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.