MolNFT v1 · #119624 · protein
Apo structure of linalool dehydratase-isomerase
5G1W · Linalool DEHYDRATASE/ISOMERASE: “Apo structure of linalool dehydratase-isomerase”. X-ray diffraction, 1 ligand (DXX), 12 pockets (best druggability 0.71). MolNFT v1 #119624 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5G1W
- Type
- protein
- Length
- 1,822 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
- DXX
- Pockets
- 12 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 364 | 57% helix, 7% strand | E1XUJ2 |
| C, E | Linalool DEHYDRATASE/ISOMERASE (EC 4.2.1.127, 5.4.4.4) | protein | 365 | 56% helix, 8% strand | E1XUJ2 |
Ligands and binding sites
- DXX · Methylmalonic acid · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 11 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.71 | 0.88 | 42 | empty |
| 2 | 175 | 0.70 | 0.88 | 32 | empty |
| 3 | 54 | 0.70 | 0.97 | 21 | empty |
| 4 | 159 | 0.68 | 0.87 | 33 | empty |
| 5 | 189 | 0.66 | 0.85 | 33 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1200 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1191 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1188 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1184 Ų buried · 12 hydrogen bonds · protein-protein
- C–E · 1175 Ų buried · 12 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 5G1W · PDBe 5G1W · UniProt E1XUJ2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.