Research workbench
Crystal structure of class ib terpene synthase bound with geranylcitronellyl diphosphate
Analyse Crystal structure of class ib terpene synthase bound with geranylcitronellyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LOO
- Type
- protein
- Length
- 694 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetraprenyl-beta-curcumene synthase
- UniProt
- A0A094YZ24
- Ligands
- ELR, ELU
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tetraprenyl-beta-curcumene synthase | protein | 347 | 73% helix, 0% strand | A0A094YZ24 |
Ligands and binding sites
- ELR · phosphono [(3~{S},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl] hydrogen phosphate · ligand · 2 copies · chains A, B
- ELU · phosphono [(3~{R},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl] hydrogen phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 689 | 0.82 | 0.86 | 65 | ELR, ELU |
| 2 | 709 | 0.81 | 0.85 | 62 | ELR |
Interfaces
1 interface between chains.
- A–B · 893 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6LOO · Crystal Structure of Class IB terpene synthase bound with geranylcitronellyl diphosphate · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A094YZ24
- Elsewhere: RCSB PDB 6LOO · PDBe 6LOO · UniProt A0A094YZ24
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