MolNFT v2 · #228557 · protein
Crystal structure of Cryo2RT Thaumatin at 296K
9FX5 · Thaumatin I: “Crystal structure of Cryo2RT Thaumatin at 296K”. X-ray diffraction at 1.592. MolNFT v2 #228557 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 9FX5
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.592
- Source
- Thaumatococcus daniellii
- Molecule
- Thaumatin I
- UniProt
- P02883
Structure
x-ray diffraction · resolution 1.592 · 1 distinct chain · 12% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thaumatin I | protein | 207 | 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).
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 9FX5 · PDBe 9FX5 · UniProt P02883
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.