Research workbench
TSC1 N-terminal domain
Analyse TSC1 N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A0M
- Type
- protein
- Length
- 1,445 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TSC1 N-terminal domain
- UniProt
- G0S5K3
- Ligands
- SO4
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TSC1 N-terminal domain | protein | 358 | 72% helix, 1% strand | G0S5K3 |
| B | TSC1 N-terminal domain | protein | 364 | 72% helix, 1% strand | G0S5K3 |
| C | TSC1 N-terminal domain | protein | 368 | 73% helix, 1% strand | G0S5K3 |
| D | TSC1 N-terminal domain | protein | 355 | 73% helix, 1% strand | G0S5K3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 494 | 0.79 | 0.86 | 41 | SO4 |
| 2 | 264 | 0.65 | 0.82 | 34 | SO4 |
| 3 | 207 | 0.51 | 0.77 | 26 | empty |
| 4 | 170 | 0.51 | 0.78 | 21 | empty |
| 5 | 163 | 0.48 | 0.77 | 24 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1015 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1009 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 316 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 315 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 20 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 7A0M · TSC1 N-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
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 G0S5K3
- Elsewhere: RCSB PDB 7A0M · PDBe 7A0M · UniProt G0S5K3
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