Research workbench
AlphaFold monomer V2.0 prediction for beta-conglycinin beta subunit 1 (P25974)
Analyse AlphaFold monomer V2.0 prediction for beta-conglycinin beta subunit 1 (P25974) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P25974
- Type
- protein
- Length
- 439 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- UniProt
- P25974
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 439 | — | P25974 |
Compared structures
- 1IPK · Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers · an experimental structure of the same protein · chain A against C, TM-score 0.86
- 1IPK · Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers · an experimental structure of the same protein · chain A against C, TM-score 0.86
- 1UIJ · Crystal structure of soybean beta-conglycinin beta homotrimer (I122M/K124W) · an experimental structure of the same protein · chain A against D, TM-score 0.86
- 1UIJ · Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W) · an experimental structure of the same protein · chain A against D, TM-score 0.86
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 P25974
- Elsewhere: UniProt P25974 · AlphaFold DB P25974
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