Research workbench
Linalool dehydratase isomerase in complex with geraniol
Analyse Linalool dehydratase isomerase in complex with geraniol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G1U
- Type
- protein
- Length
- 1,813 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
- Ligands
- 64Z
- Pockets
- 11 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 362 | 57% helix, 9% strand | E1XUJ2 |
| B | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 364 | 57% helix, 9% strand | E1XUJ2 |
| C | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 363 | 57% helix, 8% strand | E1XUJ2 |
Ligands and binding sites
- 64Z · Geraniol · ligand · 5 copies · chains A, C, B, D, E
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 | 133 | 0.68 | 0.89 | 27 | 64Z |
| 2 | 148 | 0.68 | 0.88 | 28 | 64Z |
| 3 | 147 | 0.68 | 0.88 | 28 | 64Z |
| 4 | 143 | 0.67 | 0.87 | 27 | 64Z |
| 5 | 152 | 0.66 | 0.86 | 28 | 64Z |
Interfaces
5 interfaces between chains.
- A–C · 1239 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 1236 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 1203 Ų buried · 11 hydrogen bonds · protein-protein
- C–E · 1202 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 1168 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 45 modified, 10 disulfide (engineered, 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 5G1U · PDBe 5G1U · UniProt E1XUJ2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.