Research workbench
AlphaFold monomer V2.0 prediction for insulin-like growth factor- binding protein 5 (P24593)
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
- P24593
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4bC225Cd2778aD8b434c09FeFE8BcBb702fea729
- UniProt
- P24593
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 272 | — | P24593 |
Compared structures
- 1H59 · Complex of IGFBP-5 with IGF-I · an experimental structure of the same protein · chain A against B, TM-score 0.16
- 1H59 · Complex of igfbp-5 with igf-I · an experimental structure of the same protein · chain A against B, TM-score 0.16
- 1BOE · Structure of the igf binding domain of the insulin-like growth factor-binding protein-5… · an experimental structure of the same protein · chain A against A, TM-score 0.16
- 1BOE · Structure of the igf binding domain of the insulin-like growth factor- binding protein-5… · an experimental structure of the same protein · chain A against A, TM-score 0.16
- 7UFG · Cryo-EM structure of PAPP-A in complex with IGFBP5 · an experimental structure of the same protein · chain A against D, TM-score 0.09
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 P24593
- Elsewhere: UniProt P24593 · AlphaFold DB P24593
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