Research workbench
Alpha-E-catenin abd-F-actin complex
Analyse Alpha-E-catenin abd-F-actin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UPV
- Type
- protein
- Length
- 2,201 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catenin alpha-1; Actin, alpha skeletal muscle
- UniProt
- P35221, P68139
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.76
Structure
electron microscopy · 2 distinct chains · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M, L | Catenin alpha-1 | protein | 173 | 59% helix, 0% strand | P35221 |
| A, B, C, D, E | Actin, alpha skeletal muscle | protein | 371 | 30% helix, 20% strand | P68139 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.76 | 0.88 | 53 | ADP, MG |
| 2 | 310 | 0.76 | 0.88 | 47 | ADP, MG |
| 3 | 291 | 0.76 | 0.88 | 42 | ADP, MG |
| 4 | 355 | 0.75 | 0.86 | 56 | ADP, MG |
| 5 | 495 | 0.75 | 0.83 | 51 | empty |
Interfaces
12 interfaces between chains.
- A–L · 1227 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 1199 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 1188 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1185 Ų buried · 10 hydrogen bonds · protein-protein
- M–C · 1180 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 covalent, 5 modified (covalent ligand, methylation).
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 P35221
- Every structure of UniProt P68139
- Elsewhere: RCSB PDB 6UPV · PDBe 6UPV · UniProt P35221 · UniProt P68139
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