Research workbench
NMR solution structure of the tsr domain of malaria trap protein
Analyse NMR solution structure of the tsr domain of malaria trap protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BBX
- Type
- protein
- Length
- 49 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thrombospondin-related anonymous protein
- UniProt
- P16893
Structure
solution nmr · 1 distinct chain · 0% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thrombospondin-related anonymous protein | protein | 49 | 0% helix, 20% strand | P16893 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2BBX · NMR solution structure of the TSR domain of malaria TRAP protein · the same entry in another collection · chain A against A, TM-score 1.00
- P16893 · AlphaFold monomer V2.0 prediction for thrombospondin-related anonymous protein (P16893) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 P16893
- Elsewhere: RCSB PDB 2BBX · PDBe 2BBX · UniProt P16893
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