Research workbench
AlphaFold monomer V2.0 prediction for beta-microseminoprotein (D2X5V5)
Analyse AlphaFold monomer V2.0 prediction for beta-microseminoprotein (D2X5V5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D2X5V5
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Beta-microseminoprotein
- UniProt
- D2X5V5
Structure
1 distinct chain · 4% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-microseminoprotein | protein | 91 | 4% helix, 53% strand | D2X5V5 |
Modifications
Observed in the structure: 5 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 D2X5V5
- Elsewhere: UniProt D2X5V5 · AlphaFold DB D2X5V5
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