MolNFT v1 · #45155 · protein
Shifting the polarity of some critical residues in malarial peptides binding to host cells is a key factor in breaking conserved antigens
2MUA: “Shifting the polarity of some critical residues in malarial peptides binding to host cells is a key factor in…”. Solution nmr. MolNFT v1 #45155 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
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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