Research workbench
AlphaFold monomer V2.0 prediction for melanoma-associated antigen 1 (P43355)
Analyse AlphaFold monomer V2.0 prediction for melanoma-associated antigen 1 (P43355) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P43355
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9a7859522C8b5BAa3f909CfabcF4eC23854808F5
- UniProt
- P43355
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 309 | — | P43355 |
Compared structures
- 3BO8 · The High Resolution Crystal Structure of HLA-A1 Complexed with the MAGE-A1 Peptide · an experimental structure of the same protein · chain A against C, TM-score 0.03
- 3BO8 · The high resolution crystal structure of HLA-A1 complexed with the mage-A1 peptide · an experimental structure of the same protein · chain A against C, TM-score 0.03
- 1W72 · Crystal structure of HLA-A1:MAGE-A1 in complex with Fab-Hyb3 · an experimental structure of the same protein · chain A against C, TM-score 0.02
- 1W72 · Crystal structure of HLA-A1:MAGE-A1 in complex with Fab- HYB3 · an experimental structure of the same protein · chain A against C, TM-score 0.02
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 P43355
- Elsewhere: UniProt P43355 · AlphaFold DB P43355
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