Research workbench
AlphaFold monomer V2.0 prediction for NKG2-D type II integral membrane protein (O54709)
Analyse AlphaFold monomer V2.0 prediction for NKG2-D type II integral membrane protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O54709
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc2C3F148eB26FE91165F4EE55FE4D2E3738B0950
- Molecule
- NKG2-D type II integral membrane protein
- UniProt
- O54709
Structure
1 distinct chain · 19% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NKG2-D type II integral membrane protein | protein | 232 | 19% helix, 20% strand | O54709 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4PP8 · Crystal structure of murine nk cell ligand rae-1 beta in complex with NKG2D · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 4PP8 · Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 1HQ8 · Crystal structure of the murine nk cell-activating receptor NKG2D at 1.95 a · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 1HQ8 · Crystal structure of the murine nk cell-activating receptor NKG2D at 1.95 a · an experimental structure of the same protein · chain A against A, TM-score 0.52
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 O54709
- Elsewhere: UniProt O54709 · AlphaFold DB O54709
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.