Research workbench
Crystal structure of the Nasturtium seedling xyloglucanase isoform NXG1
Analyse Crystal structure of the Nasturtium seedling xyloglucanase isoform NXG1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UWA
- Type
- protein
- Length
- 822 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- TROPAEOLUM MAJUS
- Molecule
- Cellulase
- EC
- 3.2.1.151, 3.2.1.4
- UniProt
- Q07524
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 15% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Cellulase (EC 3.2.1.151, 3.2.1.4) | protein | 274 | 15% helix, 40% strand | Q07524 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 714 | 0.76 | 0.81 | 77 | GOL |
| 2 | 160 | 0.61 | 0.84 | 27 | empty |
| 3 | 92 | 0.43 | 0.78 | 14 | empty |
| 4 | 87 | 0.40 | 0.77 | 14 | empty |
| 5 | 95 | 0.39 | 0.76 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 548 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 391 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2UWA · Crystal structure of the nasturtium seedling xyloglucanase isoform NXG1 · 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 Q07524
- Elsewhere: RCSB PDB 2UWA · PDBe 2UWA · UniProt Q07524
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