Research workbench
AlphaFold monomer V2.0 prediction for insulin-like growth factor- binding protein 7 (Q16270)
Analyse AlphaFold monomer V2.0 prediction for insulin-like growth factor- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q16270
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdD3acABBE9a72078E6d4ac1E6197192A21c69F62
- UniProt
- Q16270
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 282 | — | Q16270 |
Compared structures
- 8IVD · Complex structure of CD93-IGFBP7 · an experimental structure of the same protein · chain A against C, TM-score 0.34
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 Q16270
- Elsewhere: UniProt Q16270 · AlphaFold DB Q16270
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