Research workbench
AlphaFold monomer V2.0 prediction for alpha-aspartyl dipeptidase (Q91642)
Analyse AlphaFold monomer V2.0 prediction for alpha-aspartyl dipeptidase (Q91642) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q91642
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2815ad069368e5711A082F851Ff644B6454E18F2
- Molecule
- Alpha-aspartyl dipeptidase
- UniProt
- Q91642
Structure
1 distinct chain · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-aspartyl dipeptidase | protein | 242 | 31% helix, 21% strand | Q91642 |
Compared structures
- 7FFP · Crystal structure of di-peptidase-E from xenopus laevis · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 7FFP · Crystal structure of di-peptidase-E from Xenopus laevis · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 7C9B · Crystal structure of dipeptidase-E from xenopus laevis · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 7C9B · Crystal structure of dipeptidase-E from Xenopus laevis · an experimental structure of the same protein · chain A against A, TM-score 0.95
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 Q91642
- Elsewhere: UniProt Q91642 · AlphaFold DB Q91642
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