Research workbench
Trehalase of arabidopsis thaliana acid mutant -D380A
Analyse Trehalase of arabidopsis thaliana acid mutant -D380A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E9X
- Type
- protein
- Length
- 2,187 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trehalase
- EC
- 3.2.1.28
- UniProt
- Q9SU50
- Pockets
- 19 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trehalase (EC 3.2.1.28) | protein | 549 | 53% helix, 11% strand | Q9SU50 |
| B | Trehalase (EC 3.2.1.28) | protein | 550 | 53% helix, 11% strand | Q9SU50 |
| C | Trehalase (EC 3.2.1.28) | protein | 540 | 53% helix, 11% strand | Q9SU50 |
| D | Trehalase (EC 3.2.1.28) | protein | 548 | 53% helix, 10% strand | Q9SU50 |
Ligands and binding sites
- GOL · Glycerol · additive · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1111 | 0.85 | 0.86 | 111 | empty |
| 2 | 156 | 0.82 | 0.98 | 31 | GOL |
| 3 | 153 | 0.81 | 0.97 | 29 | GOL |
| 4 | 141 | 0.80 | 0.97 | 32 | GOL |
| 5 | 694 | 0.79 | 0.84 | 70 | empty |
Interfaces
3 interfaces between chains.
- C–D · 873 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 596 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 515 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 Q9SU50
- Elsewhere: RCSB PDB 7E9X · PDBe 7E9X · UniProt Q9SU50
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