Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized lipoprotein ygdr (P65294)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized lipoprotein ygdr (P65294) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P65294
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Uncharacterized lipoprotein ygdr
- UniProt
- P65294
Structure
1 distinct chain · 26% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized lipoprotein ygdr | protein | 72 | 26% helix, 43% strand | P65294 |
Compared structures
- 3FIF · Crystal structure of the ygdR protein from E.coli. Northeast Structural Genomics target… · an experimental structure of the same protein · chain A against C, TM-score 0.63
- 3FIF · Crystal structure of the ygdr protein from E.COLI. northeast structural genomics target… · an experimental structure of the same protein · chain A against C, TM-score 0.63
- 2JN0 · Solution NMR structure of the ygdr protein from escherichia COLI. northeast structural… · an experimental structure of the same protein · chain A against A, TM-score 0.55
- 2JN0 · Solution NMR structure of the ygdR protein from Escherichia coli. Northeast Structural… · an experimental structure of the same protein · chain A against A, TM-score 0.55
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 P65294
- Elsewhere: UniProt P65294 · AlphaFold DB P65294
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.