Research workbench
AlphaFold monomer V2.0 prediction for F-actin-capping protein subunit alpha (P13022)
Analyse AlphaFold monomer V2.0 prediction for F-actin-capping protein subunit alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P13022
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDc9c9Af88E0b0A5Ec61DD36Ae0Ecd840271f80cF
- UniProt
- P13022
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 281 | — | P13022 |
Compared structures
- 4AKR · Crystal Structure of the cytoplasmic actin capping protein Cap32_34 from Dictyostelium… · an experimental structure of the same protein · chain A against C, TM-score 0.95
- 4AKR · Crystal structure of the cytoplasmic actin capping protein CAP32_34 from dictyostelium… · an experimental structure of the same protein · chain A against C, TM-score 0.95
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 P13022
- Elsewhere: UniProt P13022 · AlphaFold DB P13022
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