Research workbench
Shifting the polarity of some critical residues in malarial peptides binding to host cells is a key factor in breaking conserved antigens
Analyse Shifting the polarity of some critical residues in malarial peptides binding to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MUA
- Type
- protein
- Length
- 21 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13830
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 21 | — | P13830 |
Compared structures
- 2MUA · Shifting the Polarity of some Critical Residues in Malarial Peptides Binding to Host… · the same entry in another collection · chain A against A, TM-score 1.00
- P13830 · AlphaFold monomer V2.0 prediction for ring-infected erythrocyte surface antigen (P13830) · a predicted model 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 P13830
- Elsewhere: RCSB PDB 2MUA · PDBe 2MUA · UniProt P13830
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