Research workbench
Tilted state of actin, T2
Analyse Tilted state of actin, T2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J8K
- Type
- protein
- Length
- 3,750 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle
- UniProt
- P68135
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Actin, alpha skeletal muscle | protein | 375 | 39% helix, 15% strand | P68135 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1123 | 0.85 | 0.85 | 127 | empty |
| 2 | 686 | 0.83 | 0.87 | 92 | empty |
| 3 | 923 | 0.79 | 0.81 | 121 | empty |
| 4 | 193 | 0.78 | 0.93 | 33 | empty |
| 5 | 901 | 0.77 | 0.80 | 99 | empty |
Interfaces
17 interfaces between chains.
- H–J · 594 Ų buried · 9 hydrogen bonds · protein-protein
- I–J · 514 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 465 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 464 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 453 Ų buried · 5 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 P68135
- Elsewhere: RCSB PDB 3J8K · PDBe 3J8K · UniProt P68135
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