Research workbench
Human 14-3-3 sigma fused to the STARD1 peptide including phosphoserine-195
Analyse Human 14-3-3 sigma fused to the STARD1 peptide including phosphoserine-195 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T5F
- Type
- protein
- Length
- 965 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma; STARD1 peptide
- UniProt
- P31947
- Pockets
- 10 · best druggability 0.69
Structure
x-ray diffraction · 7 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | 14-3-3 protein sigma | protein | 235 | 79% helix, 0% strand | P31947 |
| B | 14-3-3 protein sigma | protein | 231 | 80% helix, 0% strand | P31947 |
| D | 14-3-3 protein sigma | protein | 227 | 82% helix, 0% strand | P31947 |
| E | STARD1 peptide | protein | 10 | 0% helix, 0% strand | — |
| F | STARD1 peptide | protein | 11 | 0% helix, 0% strand | — |
| G | STARD1 peptide | protein | 7 | 0% helix, 0% strand | — |
| H | STARD1 peptide | protein | 9 | 0% helix, 0% strand | — |
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 | 267 | 0.69 | 0.84 | 31 | empty |
| 2 | 813 | 0.68 | 0.75 | 80 | empty |
| 3 | 232 | 0.62 | 0.81 | 25 | empty |
| 4 | 362 | 0.58 | 0.76 | 25 | empty |
| 5 | 364 | 0.57 | 0.75 | 24 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1126 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1055 Ų buried · 18 hydrogen bonds · protein-protein
- D–F · 642 Ų buried · 16 hydrogen bonds · protein-protein
- C–E · 618 Ų buried · 20 hydrogen bonds · protein-protein
- B–H · 529 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6T5F · Human 14-3-3 sigma fused to the StARD1 peptide including phosphoserine-195 · the same entry in another collection · chain H against H, 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 D against A, TM-score 0.98
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 6T5F · PDBe 6T5F · UniProt P31947
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