Research workbench
Crystal structure of ciboulot in complex with skeletal actin
Analyse Crystal structure of ciboulot in complex with skeletal actin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SQK
- Type
- protein
- Length
- 385 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Ciboulot
- UniProt
- P68135, O97428
- Ligands
- ADP, LAR, MG
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin, alpha skeletal muscle | protein | 360 | 45% helix, 20% strand | P68135 |
| B | Ciboulot | protein | 25 | 48% helix, 4% strand | O97428 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- LAR · Latrunculin A · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 413 | 0.71 | 0.82 | 55 | MG, ADP, LAR |
| 2 | 311 | 0.63 | 0.79 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 896 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1SQK · Crystal structure of ciboulot in complex with skeletal actin · 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 O97428
- Elsewhere: RCSB PDB 1SQK · PDBe 1SQK · UniProt P68135 · UniProt O97428
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