Research workbench
AlphaFold monomer V2.0 prediction for translocation protein SEC62 (P21825)
Analyse AlphaFold monomer V2.0 prediction for translocation protein SEC62 (P21825) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P21825
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9C80B506aC88CC4745F2CFbA143f406EBbF0Cf05
- Molecule
- Translocation protein SEC62
- UniProt
- P21825
Structure
1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translocation protein SEC62 | protein | 274 | 54% helix, 12% strand | P21825 |
Compared structures
- 6ZZZ · Crystal structure of yeast Sec62 cytoplasmic domain · an experimental structure of the same protein · chain A against A, TM-score 0.46
- 6ZZZ · Crystal structure of yeast SEC62 cytoplasmic domain · an experimental structure of the same protein · chain A against A, TM-score 0.46
- 7AFT · Cryo-EM structure of the signal sequence-engaged post-translational sec translocon · an experimental structure of the same protein · chain A against G, TM-score 0.15
- 7AFT · Cryo-EM structure of the signal sequence-engaged post-translational Sec translocon · an experimental structure of the same protein · chain A against G, TM-score 0.15
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 P21825
- Elsewhere: UniProt P21825 · AlphaFold DB P21825
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