Research workbench
AlphaFold monomer V2.0 prediction for proheparin-binding EGF-like growth factor (Q99075)
Analyse AlphaFold monomer V2.0 prediction for proheparin-binding EGF-like growth factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99075
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x422f92Ed16F3e38E0Df945A0deE92D80fCDFD0FB
- UniProt
- Q99075
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 208 | — | Q99075 |
Compared structures
- 1XDT · Complex of diphtheria toxin and heparin-binding epidermal growth factor · an experimental structure of the same protein · chain A against R, TM-score 0.19
- 1XDT · Complex of diphtheria toxin and heparin-binding epidermal growth factor · an experimental structure of the same protein · chain A against R, TM-score 0.19
- 2M8S · NMR Structure of the Cytoplasmic Tail of the Membrane Form of Heparin-binding EGF-like… · an experimental structure of the same protein · chain A against B, TM-score 0.04
- 2M8S · NMR structure of the cytoplasmic tail of the membrane form of heparin- binding EGF-like… · an experimental structure of the same protein · chain A against B, TM-score 0.04
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 Q99075
- Elsewhere: UniProt Q99075 · AlphaFold DB Q99075
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