Research workbench
AlphaFold monomer V2.0 prediction for H/ACA ribonucleoprotein complex subunit GAR1 (P28007)
Analyse AlphaFold monomer V2.0 prediction for H/ACA ribonucleoprotein complex subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28007
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE1e5aDB0467c1773e79F5F91807F3aee2545A6f9
- UniProt
- P28007
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 205 | — | P28007 |
Compared structures
- 3U28 · Crystal structure of a Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae · an experimental structure of the same protein · chain A against C, TM-score 0.44
- 3U28 · Crystal structure of a CBF5-NOP10-GAR1 complex from saccharomyces cerevisiae · an experimental structure of the same protein · chain A against C, TM-score 0.44
- 3UAI · Structure of the Shq1-Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae · an experimental structure of the same protein · chain A against C, TM-score 0.44
- 3UAI · Structure of the SHQ1-CBF5-NOP10-GAR1 complex from saccharomyces cerevisiae · an experimental structure of the same protein · chain A against C, TM-score 0.44
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 P28007
- Elsewhere: UniProt P28007 · AlphaFold DB P28007
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