Research workbench
Crystal structure of C-terminal modified tau peptide-hybrid 201D with 14-3-3SIGMA
Analyse Crystal structure of C-terminal modified tau peptide-hybrid 201D with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HF3
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; Modified tau peptide
- UniProt
- P31947
- Ligands
- ACE, 60H
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 231 | 80% helix, 0% strand | P31947 |
| B | Modified tau peptide | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, B
- 60H · (2~{S})-2-(diphenylmethyl)pyrrolidine · ligand · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.47 | 0.81 | 17 | 60H |
| 2 | 70 | 0.37 | 0.78 | 16 | empty |
| 3 | 52 | 0.34 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 574 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 modified (covalent ligand, oxidation, phosphorylation).
Compared structures
- 5HF3 · Crystal structure of C-terminal modified Tau peptide-hybrid 201D with 14-3-3sigma · 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
- Elsewhere: RCSB PDB 5HF3 · PDBe 5HF3 · UniProt P31947
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