Research workbench
AlphaFold monomer V2.0 prediction for endoplasmic reticulum vesicle protein 25 (Q5B5L5)
Analyse AlphaFold monomer V2.0 prediction for endoplasmic reticulum vesicle protein 25… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5B5L5
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8DD805493e22E8987a3BbCDFeD5cc3a28Cd35b3f
- Molecule
- Endoplasmic reticulum vesicle protein 25
- UniProt
- Q5B5L5
Structure
1 distinct chain · 44% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmic reticulum vesicle protein 25 | protein | 216 | 44% helix, 29% strand | Q5B5L5 |
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 Q5B5L5
- Elsewhere: UniProt Q5B5L5 · AlphaFold DB Q5B5L5
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