Research workbench
Evidence supporting the hypothesis that specifically modifying a malaria peptide to fit into HLA-dr 1*03 molecules induces antibody production and protection
Analyse Evidence supporting the hypothesis that specifically modifying a malaria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MTW
- Type
- protein
- Length
- 20 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19214
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 20 | — | P19214 |
Compared structures
- 2MTW · Evidence supporting the hypothesis that specifically modifying a malaria peptide to fit… · the same entry in another collection · chain A against A, TM-score 1.00
- P19214 · AlphaFold monomer V2.0 prediction for erythrocyte-binding antigen 175 (P19214) · a predicted model of the same protein · chain A against A, TM-score 0.49
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 P19214
- Elsewhere: RCSB PDB 2MTW · PDBe 2MTW · UniProt P19214
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