Research workbench
Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S
Analyse Crystal structure between actin and a protein construct containing the first… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U9Z
- Type
- protein
- Length
- 377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Ciboulot, isoform a
- UniProt
- P68135, O97428
- Ligands
- ADP, MG
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin, alpha skeletal muscle | protein | 357 | 44% helix, 19% strand | P68135 |
| C | Ciboulot, isoform a | protein | 20 | 45% helix, 5% strand | O97428 |
Ligands and binding sites
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 | 359 | 0.72 | 0.84 | 56 | ADP, MG |
| 2 | 240 | 0.54 | 0.77 | 32 | empty |
Interfaces
1 interface between chains.
- A–C · 807 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3U9Z · Crystal structure between actin and a protein construct containing the first… · 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 0.97
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 3U9Z · PDBe 3U9Z · UniProt P68135 · UniProt O97428
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