Research workbench
AlphaFold monomer V2.0 prediction for RING1 and YY1-binding protein (Q8N488)
Analyse AlphaFold monomer V2.0 prediction for RING1 and YY1-binding protein (Q8N488) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8N488
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x644EE9f2182e8e21d43CdeF48634b74F602D9E42
- Molecule
- RING1 and YY1-binding protein
- UniProt
- Q8N488
Structure
1 distinct chain · 7% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RING1 and YY1-binding protein | protein | 228 | 7% helix, 11% strand | Q8N488 |
Compared structures
- 3IXS · Ring1B C-terminal domain/RYBP C-terminal domain Complex · an experimental structure of the same protein · chain A against H, TM-score 0.16
- 3IXS · RING1B C-terminal DOMAIN/RYBP C-terminal domain complex · an experimental structure of the same protein · chain A against H, TM-score 0.16
- 9DBY · ncPRC1RYBP bound to singly modified H2AK119Ub nucleosome · an experimental structure of the same protein · chain A against M, TM-score 0.13
- 9DDE · ncPRC1RYBP bound to H2AK119Ub/H1.4 chromatosome · an experimental structure of the same protein · chain A against M, TM-score 0.13
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 Q8N488
- Elsewhere: UniProt Q8N488 · AlphaFold DB Q8N488
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