Research workbench
Linalool dehydratase isomerase G107T mutant
Analyse Linalool dehydratase isomerase G107T mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AD2
- Type
- protein
- Length
- 1,824 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Linalool DEHYDRATASE/ISOMERASE
- EC
- 4.2.1.127, 5.4.4.4
- UniProt
- E1XUJ2
- Pockets
- 11 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 56% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 364 | 57% helix, 8% strand | E1XUJ2 |
| C, E | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 365 | 56% helix, 7% strand | E1XUJ2 |
| D | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 366 | 56% helix, 8% strand | E1XUJ2 |
Ligands and binding sites
- MLI · Malonate ion · additive · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.68 | 0.88 | 25 | empty |
| 2 | 121 | 0.66 | 0.88 | 25 | empty |
| 3 | 149 | 0.66 | 0.86 | 26 | empty |
| 4 | 144 | 0.65 | 0.86 | 25 | empty |
| 5 | 159 | 0.65 | 0.85 | 26 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1205 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1204 Ų buried · 14 hydrogen bonds · protein-protein
- B–E · 1201 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 1193 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 1192 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
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 E1XUJ2
- Elsewhere: RCSB PDB 7AD2 · PDBe 7AD2 · UniProt E1XUJ2
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