Research workbench
AlphaFold monomer V2.0 prediction for parvalbumin beta (P56503)
Analyse AlphaFold monomer V2.0 prediction for parvalbumin beta (P56503) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P56503
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcF3444A9d2FD68005aA0248bc2E47C278EDb79C8
- Molecule
- Parvalbumin beta
- UniProt
- P56503
Structure
1 distinct chain · 56% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parvalbumin beta | protein | 108 | 56% helix, 6% strand | P56503 |
Compared structures
- 1BU3 · Refined crystal structure of calcium-bound silver hake (pi 4.2) parvalbumin at 1.65 a. · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 1BU3 · Refined crystal structure of calcium-bound silver hake (pi 4.2) parvalbumin at 1.65 a. · an experimental structure of the same protein · chain A against A, TM-score 0.96
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 P56503
- Elsewhere: UniProt P56503 · AlphaFold DB P56503
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