Research workbench
Deciphering the design of the tropomyosin molecule
Analyse Deciphering the design of the tropomyosin molecule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IC2
- Type
- protein
- Length
- 312 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tropomyosin alpha chain, skeletal muscle
- UniProt
- P04268
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 95% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Tropomyosin alpha chain, skeletal muscle | protein | 79 | 95% helix, 0% strand | P04268 |
| B, D | Tropomyosin alpha chain, skeletal muscle | protein | 77 | 95% helix, 0% strand | P04268 |
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 | 210 | 0.46 | 0.74 | 27 | empty |
| 2 | 107 | 0.36 | 0.74 | 15 | empty |
| 3 | 70 | 0.29 | 0.73 | 15 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2036 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 2025 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 314 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 197 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 18 Ų buried · 0 hydrogen bonds · 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 P04268
- Elsewhere: RCSB PDB 1IC2 · PDBe 1IC2 · UniProt P04268
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