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Crystal structure of the rod domain of alpha-actinin
Analyse Crystal structure of the rod domain of alpha-actinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HCI
- Type
- protein
- Length
- 950 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-actinin 2
- UniProt
- P35609
- Pockets
- 14 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-actinin 2 | protein | 475 | 78% helix, 0% strand | P35609 |
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 402 | 0.61 | 0.76 | 48 | empty |
| 2 | 283 | 0.56 | 0.76 | 34 | empty |
| 3 | 228 | 0.54 | 0.77 | 29 | empty |
| 4 | 178 | 0.52 | 0.78 | 25 | empty |
| 5 | 163 | 0.50 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 3456 Ų buried · 21 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 P35609
- Elsewhere: RCSB PDB 1HCI · PDBe 1HCI · UniProt P35609
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