Research workbench
W203Y epi-isozizaene synthase
Analyse W203Y epi-isozizaene synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AXU
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epi-isozizaene synthase
- EC
- 4.2.3.37
- UniProt
- Q9K499
- Ligands
- BTM, POP, MG
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epi-isozizaene synthase (EC 4.2.3.37) | protein | 340 | 75% helix, 0% strand | Q9K499 |
Ligands and binding sites
- BTM · N-benzyl-N,N-diethylethanaminium · ligand · chains A
- POP · Pyrophosphate 2- · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.84 | 0.96 | 45 | BTM, POP, MG |
| 2 | 53 | 0.42 | 0.83 | 17 | empty |
| 3 | 61 | 0.34 | 0.77 | 12 | empty |
| 4 | 57 | 0.28 | 0.74 | 15 | 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 Q9K499
- Elsewhere: RCSB PDB 6AXU · PDBe 6AXU · UniProt Q9K499
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