Research workbench
The structure of crystalline profilin-beta-actin
Analyse The structure of crystalline profilin-beta-actin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BTF
- Type
- protein
- Length
- 513 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-actin; Profilin
- UniProt
- P60712, P02584
- Ligands
- ACE, ATP, SR
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-actin | protein | 374 | 41% helix, 19% strand | P60712 |
| P | Profilin | protein | 139 | 27% helix, 31% strand | P02584 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, P
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- SR · Strontium 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 | 373 | 0.74 | 0.85 | 50 | SR, ATP |
| 2 | 461 | 0.71 | 0.81 | 59 | empty |
Interfaces
1 interface between chains.
- A–P · 1085 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 1 modified (covalent ligand, methylation).
Compared structures
- 2BTF · The structure of crystalline profilin-beta-actin · the same entry in another collection · chain A against A, TM-score 1.00
- P02584 · AlphaFold monomer V2.0 prediction for profilin-1 (P02584) · a predicted model of the same protein · chain P against A, TM-score 0.99
- P60712 · AlphaFold monomer V2.0 prediction for actin, cytoplasmic 1 (P60712) · 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 P60712
- Every structure of UniProt P02584
- Elsewhere: RCSB PDB 2BTF · PDBe 2BTF · UniProt P60712 · UniProt P02584
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