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Isolated cofilin bound to an actin filament
Analyse Isolated cofilin bound to an actin filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UBY
- Type
- protein
- Length
- 2,740 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Cofilin-1
- UniProt
- P68135, P23528
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 4 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Actin, alpha skeletal muscle | protein | 370 | 40% helix, 18% strand | P68135 |
| G | Actin, alpha skeletal muscle | protein | 190 | 43% helix, 15% strand | P68135 |
| H | Actin, alpha skeletal muscle | protein | 166 | 40% helix, 22% strand | P68135 |
| I | Cofilin-1 | protein | 164 | 27% helix, 28% strand | P23528 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 7 copies · chains A, B, C, D, E, F, G, H
- MG · Magnesium ion · metal · 7 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.85 | 0.87 | 103 | MG, ADP |
| 2 | 1091 | 0.81 | 0.82 | 94 | empty |
| 3 | 860 | 0.78 | 0.81 | 83 | empty |
| 4 | 747 | 0.77 | 0.81 | 72 | empty |
| 5 | 262 | 0.76 | 0.89 | 51 | MG, ADP |
Interfaces
19 interfaces between chains.
- A–I · 1295 Ų buried · 64 hydrogen bonds · protein-protein
- A–B · 1223 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 1200 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 1193 Ų buried · 7 hydrogen bonds · protein-protein
- G–H · 1039 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 isopeptide (isopeptide).
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 P68135
- Every structure of UniProt P23528
- Elsewhere: RCSB PDB 6UBY · PDBe 6UBY · UniProt P68135 · UniProt P23528
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