MolNFT v1 · #185488 · protein
Structure of pathological tdp-43 filaments from als with ftld
7PY2 · Tar DNA-binding protein 43: “Structure of pathological tdp-43 filaments from als with ftld”. Electron microscopy, 1 pocket (best druggability 0.32). MolNFT v1 #185488 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7PY2
- Type
- protein
- Length
- 316 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tar DNA-binding protein 43
- UniProt
- Q13148
- Pockets
- 1 · best druggability 0.32
Structure
electron microscopy · 1 distinct chain · 0% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Tar DNA-binding protein 43 | protein | 79 | 0% helix, 41% strand | Q13148 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.32 | 0.77 | 20 | empty |
Interfaces
5 interfaces between chains.
- A–B · 3410 Ų buried · 107 hydrogen bonds · protein-protein
- A–D · 3407 Ų buried · 107 hydrogen bonds · protein-protein
- C–D · 3400 Ų buried · 107 hydrogen bonds · protein-protein
- A–C · 438 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 438 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 Q13148
- Elsewhere: RCSB PDB 7PY2 · PDBe 7PY2 · UniProt Q13148
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