Research workbench
Crystal structure of human 14-3-3 sigma in complex with a tau-protein peptide surrounding PS214
Analyse Crystal structure of human 14-3-3 sigma in complex with a tau-protein peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FL5
- Type
- protein
- Length
- 472 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Microtubule-associated protein tau
- UniProt
- P31947, P10636
- Ligands
- CA, MG, CL
- Pockets
- 3 · best druggability 0.51
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 | protein | 230 | 82% helix, 0% strand | P31947 |
| B | 14-3-3 protein sigma | protein | 229 | 84% helix, 0% strand | P31947 |
| P | Microtubule-associated protein tau | protein | 8 | 0% helix, 0% strand | P10636 |
| Q | Microtubule-associated protein tau | protein | 5 | 0% helix, 0% strand | P10636 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 320 | 0.51 | 0.73 | 31 | empty |
| 2 | 131 | 0.49 | 0.79 | 22 | empty |
| 3 | 53 | 0.29 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–P · 643 Ų buried · 13 hydrogen bonds · protein-protein
- B–Q · 420 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 181 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation, phosphorylation).
Compared structures
- 4FL5 · Crystal structure of human 14-3-3 sigma in complex with a Tau-protein peptide surrounding… · 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
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 P10636
- Elsewhere: RCSB PDB 4FL5 · PDBe 4FL5 · UniProt P31947 · UniProt P10636
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