Research workbench
Structure of the TSC2 N-terminus
Analyse Structure of the TSC2 N-terminus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HIU
- Type
- protein
- Length
- 1,617 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase activator-like protein
- UniProt
- G0SFF5
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase activator-like protein | protein | 407 | 75% helix, 0% strand | G0SFF5 |
| B | GTPase activator-like protein | protein | 407 | 75% helix, 0% strand | G0SFF5 |
| C | GTPase activator-like protein | protein | 402 | 73% helix, 1% strand | G0SFF5 |
| D | GTPase activator-like protein | protein | 401 | 73% helix, 1% strand | G0SFF5 |
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 932 | 0.70 | 0.75 | 76 | empty |
| 2 | 373 | 0.60 | 0.77 | 38 | empty |
| 3 | 152 | 0.48 | 0.77 | 20 | empty |
| 4 | 104 | 0.46 | 0.79 | 17 | empty |
| 5 | 139 | 0.44 | 0.76 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–B · 564 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 537 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 428 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 346 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 106 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5HIU · Structure of the TSC2 N-terminus · 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 G0SFF5
- Elsewhere: RCSB PDB 5HIU · PDBe 5HIU · UniProt G0SFF5
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