Research workbench
Complex of mammalian actin with toxofilin from toxoplasma gondii
Analyse Complex of mammalian actin with toxofilin from toxoplasma gondii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q97
- Type
- protein
- Length
- 463 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Toxofilin
- UniProt
- P68135, Q9NG25
- Ligands
- ATP, CA
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin, alpha skeletal muscle | protein | 354 | 44% helix, 21% strand | P68135 |
| T | Toxofilin | protein | 109 | 65% helix, 0% strand | Q9NG25 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 342 | 0.77 | 0.88 | 49 | CA, ATP |
| 2 | 323 | 0.60 | 0.77 | 35 | empty |
| 3 | 96 | 0.40 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–T · 1857 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 2Q97 · Complex of mammalian actin with toxofilin from toxoplasma gondii · the same entry in another collection · chain A against A, TM-score 1.00
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9NG25
- Elsewhere: RCSB PDB 2Q97 · PDBe 2Q97 · UniProt P68135 · UniProt Q9NG25
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