Research workbench
Recombinant thaumatin in the presence of 1.5M pst at 293K
Analyse Recombinant thaumatin in the presence of 1.5M pst at 293K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XVB
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thaumatin I
- UniProt
- Q8RVT0
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thaumatin I | protein | 207 | 12% helix, 40% strand | Q8RVT0 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 4XVB · Recombinant thaumatin in the presence of 1.5M PST at 293K · 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 Q8RVT0
- Elsewhere: RCSB PDB 4XVB · PDBe 4XVB · UniProt Q8RVT0
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