Research workbench
Actin filament model from extended form of acromsomal bundle in the limulus sperm
Analyse Actin filament model from extended form of acromsomal bundle in the limulus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B5U
- Type
- protein
- Length
- 5,250 residues
- Chains
- 14
- Method
- electron crystallography
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle
- UniProt
- P68135
- Pockets
- 20 · best druggability 0.86
Structure
electron crystallography · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | Actin, alpha skeletal muscle | protein | 375 | 38% helix, 16% 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 | 969 | 0.86 | 0.88 | 131 | empty |
| 2 | 661 | 0.83 | 0.87 | 94 | empty |
| 3 | 908 | 0.80 | 0.82 | 115 | empty |
| 4 | 560 | 0.79 | 0.85 | 81 | empty |
| 5 | 289 | 0.78 | 0.89 | 45 | empty |
Interfaces
25 interfaces between chains.
- E–F · 2116 Ų buried · 51 hydrogen bonds · protein-protein
- M–N · 1253 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 1171 Ų buried · 23 hydrogen bonds · protein-protein
- K–L · 1170 Ų buried · 27 hydrogen bonds · protein-protein
- J–L · 1087 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3B5U · Actin filament model from extended form of acromsomal bundle in the Limulus sperm · the same entry in another collection · chain N against N, 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 P68135
- Elsewhere: RCSB PDB 3B5U · PDBe 3B5U · UniProt P68135
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