Research workbench
Leishmania major actin filament in ADP-state
Analyse Leishmania major actin filament in ADP-state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q8C
- Type
- protein
- Length
- 1,850 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin
- UniProt
- Q9U1E8
- Ligands
- ADP, MG
- Pockets
- 19 · best druggability 0.81
Structure
electron microscopy · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Actin | protein | 370 | 42% helix, 21% strand | Q9U1E8 |
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
19 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 753 | 0.81 | 0.84 | 80 | empty |
| 2 | 418 | 0.80 | 0.89 | 58 | ADP, MG |
| 3 | 463 | 0.80 | 0.87 | 64 | ADP, MG |
| 4 | 418 | 0.79 | 0.88 | 59 | ADP, MG |
| 5 | 388 | 0.78 | 0.87 | 52 | ADP, MG |
Interfaces
7 interfaces between chains.
- C–D · 1203 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1201 Ų buried · 13 hydrogen bonds · protein-protein
- A–E · 1201 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 447 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 446 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7Q8C · Leishmania major actin filament in ADP-state · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9U1E8
- Elsewhere: RCSB PDB 7Q8C · PDBe 7Q8C · UniProt Q9U1E8
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