Research workbench
F-actin-utrophin complex
Analyse F-actin-utrophin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M5G
- Type
- protein
- Length
- 2,204 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Utrophin
- UniProt
- P68139, P46939
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Actin, alpha skeletal muscle | protein | 370 | 39% helix, 18% strand | P68139 |
| F, G, H | Utrophin | protein | 118 | 59% helix, 0% strand | P46939 |
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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 878 | 0.81 | 0.83 | 104 | empty |
| 2 | 309 | 0.78 | 0.90 | 46 | MG, ADP |
| 3 | 340 | 0.77 | 0.88 | 53 | MG, ADP |
| 4 | 280 | 0.77 | 0.89 | 45 | MG, ADP |
| 5 | 465 | 0.74 | 0.83 | 71 | MG, ADP |
Interfaces
13 interfaces between chains.
- C–H · 1414 Ų buried · 18 hydrogen bonds · protein-protein
- B–F · 1406 Ų buried · 21 hydrogen bonds · protein-protein
- A–G · 1364 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1194 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 1172 Ų buried · 10 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 P68139
- Every structure of UniProt P46939
- Elsewhere: RCSB PDB 6M5G · PDBe 6M5G · UniProt P68139 · UniProt P46939
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