Research workbench
5-epi-aristolochene synthase from nicotiana tabacum
Analyse 5-epi-aristolochene synthase from nicotiana tabacum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EAU
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-epi-aristolochene synthase
- UniProt
- Q40577
- Ligands
- FFF, MG
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-epi-aristolochene synthase | protein | 523 | 72% helix, 0% strand | Q40577 |
Ligands and binding sites
- FFF · Trifluorofurnesyl diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.81 | 0.87 | 49 | empty |
| 2 | 667 | 0.80 | 0.84 | 64 | MG, FFF |
| 3 | 344 | 0.62 | 0.78 | 32 | empty |
| 4 | 205 | 0.58 | 0.80 | 27 | empty |
| 5 | 82 | 0.46 | 0.81 | 16 | empty |
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 Q40577
- Elsewhere: RCSB PDB 5EAU · PDBe 5EAU · UniProt Q40577
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