Research workbench
AlphaFold monomer V2.0 prediction for epsin-1 (Q12518)
Analyse AlphaFold monomer V2.0 prediction for epsin-1 (Q12518) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12518
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- UniProt
- Q12518
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 454 | — | Q12518 |
Compared structures
- 7B2L · Structure of the endocytic adaptor complex AENTH · an experimental structure of the same protein · chain A against A, TM-score 0.32
- 7B2L · Structure of the endocytic adaptor complex aenth · an experimental structure of the same protein · chain A against A, TM-score 0.32
- 5AHV · Cryo-EM structure of helical anth and enth tubules on PI(4,5)P2- containing membranes · an experimental structure of the same protein · chain A against E, TM-score 0.32
- 5AHV · Cryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranes · an experimental structure of the same protein · chain A against E, TM-score 0.32
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 Q12518
- Elsewhere: UniProt Q12518 · AlphaFold DB Q12518
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