Research workbench
Structure of recombinant thaumatin in the presence of 1.0M pst, PH7 at 293K
Analyse Structure of recombinant thaumatin in the presence of 1.0M pst, PH7 at 293K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3X3Q
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thaumatin I
- UniProt
- A1IIJ1
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thaumatin I | protein | 207 | 12% helix, 39% strand | A1IIJ1 |
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
- 3X3Q · Structure of recombinant thaumatin in the presence of 1.0M PST, pH7 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 A1IIJ1
- Elsewhere: RCSB PDB 3X3Q · PDBe 3X3Q · UniProt A1IIJ1
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