Research workbench
Structural basis of alphae-catenin - F-actin catch bond behavior
Analyse Structural basis of alphae-catenin - F-actin catch bond behavior in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WVT
- Type
- protein
- Length
- 3,240 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Catenin alpha-1
- UniProt
- P68135, P26231
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 2 distinct chains · 44% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, D, E, F, H, I | Actin, alpha skeletal muscle | protein | 372 | 37% helix, 18% strand | P68135 |
| K, L, N, O, Q, X | Catenin alpha-1 | protein | 168 | 60% helix, 0% strand | P26231 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains B, D, E, F, H, I
- MG · Magnesium ion · metal · 6 copies · chains B, D, E, F, H, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1119 | 0.83 | 0.84 | 106 | empty |
| 2 | 623 | 0.79 | 0.84 | 66 | empty |
| 3 | 523 | 0.78 | 0.85 | 54 | empty |
| 4 | 296 | 0.74 | 0.87 | 54 | MG, ADP |
| 5 | 367 | 0.73 | 0.84 | 56 | MG, ADP |
Interfaces
23 interfaces between chains.
- H–I · 1283 Ų buried · 7 hydrogen bonds · protein-protein
- B–I · 1278 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 1276 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 1265 Ų buried · 7 hydrogen bonds · protein-protein
- B–N · 1261 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (methylation).
Compared structures
- 6WVT · Structural basis of alphaE-catenin - F-actin catch bond behavior · the same entry in another collection · chain X against X, 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
- Every structure of UniProt P26231
- Elsewhere: RCSB PDB 6WVT · PDBe 6WVT · UniProt P68135 · UniProt P26231
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