Research workbench
Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain
Analyse Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ANU
- Type
- protein
- Length
- 3,048 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, cytoplasmic 1; Spectrin beta chain, non-erythrocytic 2
- UniProt
- P60709, O15020
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 2 distinct chains · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, A, B, C, D, E | Actin, cytoplasmic 1 | protein | 375 | 38% helix, 17% strand | P60709 |
| f, a, b, c, d, e | Spectrin beta chain, non-erythrocytic 2 | protein | 133 | 59% helix, 0% strand | O15020 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 725 | 0.79 | 0.83 | 81 | empty |
| 2 | 693 | 0.79 | 0.84 | 82 | empty |
| 3 | 676 | 0.79 | 0.84 | 87 | empty |
| 4 | 407 | 0.73 | 0.83 | 45 | empty |
| 5 | 356 | 0.71 | 0.83 | 48 | empty |
Interfaces
19 interfaces between chains.
- A–a · 1677 Ų buried · 42 hydrogen bonds · protein-protein
- E–e · 1677 Ų buried · 42 hydrogen bonds · protein-protein
- B–b · 1677 Ų buried · 42 hydrogen bonds · protein-protein
- D–d · 1676 Ų buried · 42 hydrogen bonds · protein-protein
- F–f · 1674 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 6ANU · Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain · the same entry in another collection · chain e against e, 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 P60709
- Every structure of UniProt O15020
- Elsewhere: RCSB PDB 6ANU · PDBe 6ANU · UniProt P60709 · UniProt O15020
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