Research workbench
Structure of thaumatin collected from an in situ crystal on ID30B at 17.5 kev.
Analyse Structure of thaumatin collected from an in situ crystal on ID30B at 17.5 kev. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FJ9
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thaumatin-1
- UniProt
- P02883
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thaumatin-1 | protein | 206 | 12% helix, 39% strand | P02883 |
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
- 6FJ9 · Structure of Thaumatin collected from an in situ crystal on ID30B at 17.5 keV. · 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 P02883
- Elsewhere: RCSB PDB 6FJ9 · PDBe 6FJ9 · UniProt P02883
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