MolNFT v1 · #167099 · protein
Human cofilin-1 decorated actin filament
6VAO · Actin, alpha skeletal muscle: “Human cofilin-1 decorated actin filament”. Electron microscopy, 2 ligands (ADP, MG), 20 pockets (best druggability 0.84). MolNFT v1 #167099 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VAO
- Type
- protein
- Length
- 2,600 residues
- Chains
- 10
- 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 0.84
Structure
electron microscopy · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A, B, C, E | Actin, alpha skeletal muscle | protein | 356 | 41% helix, 19% strand | P68135 |
| J, F, G, H, I | Cofilin-1 | protein | 164 | 27% helix, 29% strand | P23528 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains D, A, B, C, E
- MG · Magnesium ion · metal · 5 copies · chains D, A, B, C, 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, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 938 | 0.84 | 0.86 | 101 | MG, ADP |
| 2 | 967 | 0.84 | 0.85 | 109 | MG, ADP |
| 3 | 818 | 0.81 | 0.84 | 77 | empty |
| 4 | 237 | 0.78 | 0.92 | 41 | MG, ADP |
| 5 | 881 | 0.77 | 0.80 | 92 | MG, ADP |
Interfaces
15 interfaces between chains.
- D–G · 1123 Ų buried · 9 hydrogen bonds · protein-protein
- A–I · 1104 Ų buried · 7 hydrogen bonds · protein-protein
- H–E · 1098 Ų buried · 7 hydrogen bonds · protein-protein
- J–C · 1095 Ų buried · 8 hydrogen bonds · protein-protein
- E–I · 881 Ų buried · 13 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 P68135
- Every structure of UniProt P23528
- Elsewhere: RCSB PDB 6VAO · PDBe 6VAO · UniProt P68135 · UniProt P23528
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