Research workbench
Cryo-EM structure of chicken gizzard smooth muscle alpha-actinin
Analyse Cryo-EM structure of chicken gizzard smooth muscle alpha-actinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SJJ
- Type
- protein
- Length
- 1,726 residues
- Chains
- 2
- Method
- electron crystallography
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actinin
- UniProt
- P05094
- Pockets
- 20 · best druggability 0.75
Structure
electron crystallography · 1 distinct chain · 63% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Actinin | protein | 863 | 63% helix, 2% strand | P05094 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 987 | 0.75 | 0.78 | 79 | empty |
| 2 | 717 | 0.74 | 0.79 | 67 | empty |
| 3 | 609 | 0.71 | 0.79 | 50 | empty |
| 4 | 617 | 0.67 | 0.76 | 59 | empty |
| 5 | 261 | 0.63 | 0.81 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 5340 Ų buried · 90 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 P05094
- Elsewhere: RCSB PDB 1SJJ · PDBe 1SJJ · UniProt P05094
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