Research workbench
AlphaFold monomer V2.0 prediction for FAD-linked sulfhydryl oxidase ERV2 (Q12284)
Analyse AlphaFold monomer V2.0 prediction for FAD-linked sulfhydryl oxidase ERV2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12284
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- UniProt
- Q12284
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 196 | — | Q12284 |
Compared structures
- 1JRA · Crystal structure of ERV2P · an experimental structure of the same protein · chain A against B, TM-score 0.53
- 1JRA · Crystal Structure of Erv2p · an experimental structure of the same protein · chain A against B, TM-score 0.53
- 1JR8 · Crystal structure of ERV2P · an experimental structure of the same protein · chain A against B, TM-score 0.53
- 1JR8 · Crystal Structure of Erv2p · an experimental structure of the same protein · chain A against B, TM-score 0.53
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 Q12284
- Elsewhere: UniProt Q12284 · AlphaFold DB Q12284
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