Research workbench
Isolated S3D-cofilin bound to an actin filament
Analyse Isolated S3D-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
- 6UC0
- Type
- protein
- Length
- 2,754 residues
- Chains
- 8
- 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 0.83
Structure
electron microscopy · 2 distinct chains · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Actin, alpha skeletal muscle | protein | 370 | 40% helix, 18% strand | P68135 |
| I | Cofilin-1 | protein | 164 | 27% helix, 29% strand | P23528 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 7 copies · chains A, B, C, D, E, F, G
- MG · Magnesium ion · metal · 7 copies · chains A, B, C, D, E, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1018 | 0.83 | 0.84 | 110 | empty |
| 2 | 1004 | 0.83 | 0.84 | 114 | empty |
| 3 | 1065 | 0.81 | 0.82 | 111 | MG, ADP |
| 4 | 555 | 0.77 | 0.84 | 62 | empty |
| 5 | 265 | 0.76 | 0.89 | 50 | MG, ADP |
Interfaces
13 interfaces between chains.
- C–D · 1258 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1254 Ų buried · 8 hydrogen bonds · protein-protein
- E–G · 1253 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1251 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 1241 Ų buried · 8 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 6UC0 · PDBe 6UC0 · UniProt P68135 · UniProt P23528
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