Research workbench
AlphaFold monomer V2.0 prediction for tpa-induced transmembrane protein (Q5BVD1)
Analyse AlphaFold monomer V2.0 prediction for tpa-induced transmembrane protein (Q5BVD1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5BVD1
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Tpa-induced transmembrane protein
- UniProt
- Q5BVD1
Structure
1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tpa-induced transmembrane protein | protein | 217 | 37% helix, 17% strand | Q5BVD1 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q5BVD1
- Elsewhere: UniProt Q5BVD1 · AlphaFold DB Q5BVD1
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