Research workbench
Crystal structure of plant sesterterpene synthase ATTPS18 complexed with farnesyl thiolodiphosphate (fspp)
Analyse Crystal structure of plant sesterterpene synthase ATTPS18 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BZC
- Type
- protein
- Length
- 535 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Terpenoid synthase 18
- EC
- 4.2.3.-
- UniProt
- Q9LUE2
- Ligands
- FPS, MG
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Terpenoid synthase 18 (EC 4.2.3.-) | protein | 535 | 74% helix, 1% strand | Q9LUE2 |
Ligands and binding sites
- FPS · S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl] trihydrogen thiodiphosphate · 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
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.84 | 0.90 | 50 | MG, FPS |
| 2 | 304 | 0.61 | 0.79 | 30 | empty |
| 3 | 172 | 0.61 | 0.83 | 33 | empty |
| 4 | 193 | 0.54 | 0.79 | 23 | empty |
| 5 | 122 | 0.49 | 0.80 | 27 | empty |
Compared structures
- 7BZC · Crystal structure of plant sesterterpene synthase AtTPS18 complexed with farnesyl… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LUE2 · AlphaFold monomer V2.0 prediction for terpenoid synthase 18 (Q9LUE2) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9LUE2
- Elsewhere: RCSB PDB 7BZC · PDBe 7BZC · UniProt Q9LUE2
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