Research workbench
AlphaFold monomer V2.0 prediction for H-2 class II histocompatibility antigen, a-K alpha chain (P01910)
Analyse AlphaFold monomer V2.0 prediction for H-2 class II histocompatibility antigen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P01910
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- UniProt
- P01910
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 256 | — | P01910 |
Compared structures
- 1D9K · Crystal structure of complex between D10 TCR and pmhc I-AK/CA · an experimental structure of the same protein · chain A against C, TM-score 0.70
- 1D9K · Crystal structure of complex between D10 TCR and pmhc I-AK/CA · an experimental structure of the same protein · chain A against C, TM-score 0.70
- 1IAK · Histocompatibility antigen I-ak · an experimental structure of the same protein · chain A against A, TM-score 0.69
- 1IAK · Histocompatibility antigen I-ak · an experimental structure of the same protein · chain A against A, TM-score 0.69
- 1JL4 · Crystal structure of the human CD4 N-terminal two domain fragment complexed to a class II… · an experimental structure of the same protein · chain A against A, TM-score 0.68
- 1JL4 · Crystal structure of the human CD4 N-terminal two domain fragment complexed to a class II… · an experimental structure of the same protein · chain A against A, TM-score 0.68
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 P01910
- Elsewhere: UniProt P01910 · AlphaFold DB P01910
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