Research workbench
R304K trichodiene synthase
Analyse R304K trichodiene synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AEK
- Type
- protein
- Length
- 708 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trichodiene synthase
- EC
- 4.2.3.6
- UniProt
- P13513
- Ligands
- MG
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trichodiene synthase (EC 4.2.3.6) | protein | 354 | 72% helix, 0% strand | P13513 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 546 | 0.77 | 0.84 | 49 | MG, EDO |
| 2 | 544 | 0.77 | 0.84 | 56 | MG, EDO |
| 3 | 126 | 0.51 | 0.81 | 24 | empty |
| 4 | 116 | 0.50 | 0.80 | 19 | empty |
| 5 | 105 | 0.49 | 0.81 | 20 | 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 P13513
- Elsewhere: RCSB PDB 2AEK · PDBe 2AEK · UniProt P13513
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