Research workbench
Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin
Analyse Cryogenic electron microscopy 3D map of F-actin bound by human dimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UTJ
- Type
- protein
- Length
- 3,156 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.77
- Source
- Homo sapiens; Oryctolagus cuniculus
- Molecule
- Actin, alpha skeletal muscle; Catenin alpha-1
- UniProt
- P68135, P35221
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.74
Structure
electron microscopy · resolution 2.77 · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Actin, alpha skeletal muscle | protein | 370 | 43% helix, 21% strand | P68135 |
| G, H, I, K, L, Z | Catenin alpha-1 | protein | 156 | 72% helix, 0% strand | P35221 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F
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 | 360 | 0.74 | 0.85 | 56 | ADP, MG |
| 2 | 262 | 0.74 | 0.88 | 46 | ADP, MG |
| 3 | 364 | 0.73 | 0.85 | 56 | ADP, MG |
| 4 | 365 | 0.73 | 0.84 | 59 | ADP, MG |
| 5 | 352 | 0.73 | 0.85 | 52 | ADP, MG |
Interfaces
23 interfaces between chains.
- A–H · 1307 Ų buried · 10 hydrogen bonds · protein-protein
- C–Z · 1300 Ų buried · 10 hydrogen bonds · protein-protein
- E–L · 1296 Ų buried · 8 hydrogen bonds · protein-protein
- B–I · 1288 Ų buried · 9 hydrogen bonds · protein-protein
- D–K · 1278 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (methylation).
Compared structures
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain E against A, TM-score 0.96
- P35221 · AlphaFold monomer V2.0 prediction for catenin alpha-1 (P35221) · a predicted model of the same protein · chain H against A, TM-score 0.76
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 P35221
- Elsewhere: RCSB PDB 7UTJ · PDBe 7UTJ · UniProt P68135 · UniProt P35221
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