Research workbench
Crystal structure of D383A mutant from Arabidopsis thaliana complexed with Galactose.
Analyse Crystal structure of D383A mutant from Arabidopsis thaliana complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EXG
- Type
- protein
- Length
- 1,432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Arabidopsis thaliana
- Molecule
- Probable galactinol--sucrose galactosyltransferase 6
- EC
- 2.4.1.82
- UniProt
- Q8RX87
- Ligands
- GAL
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · resolution 2.05 · 1 distinct chain · 23% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Probable galactinol--sucrose galactosyltransferase 6 (EC 2.4.1.82) | protein | 716 | 23% helix, 36% strand | Q8RX87 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.72 | 0.97 | 26 | empty |
| 2 | 741 | 0.69 | 0.76 | 61 | empty |
| 3 | 238 | 0.55 | 0.77 | 36 | GAL |
| 4 | 200 | 0.52 | 0.77 | 31 | GAL |
| 5 | 195 | 0.47 | 0.75 | 26 | empty |
Interfaces
1 interface between chains.
- B–A · 1428 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- Q8RX87 · AlphaFold monomer V2.0 prediction for probable galactinol--sucrose galactosyltransferase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q8RX87
- Elsewhere: RCSB PDB 7EXG · PDBe 7EXG · UniProt Q8RX87
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