Research workbench
F95Y epi-isozizaene synthase
Analyse F95Y 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
- 6AXM
- 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
- POP, BTM, MG
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epi-isozizaene synthase (EC 4.2.3.37) | protein | 340 | 76% helix, 0% strand | Q9K499 |
Ligands and binding sites
- POP · Pyrophosphate 2- · ligand · chains A
- BTM · N-benzyl-N,N-diethylethanaminium · 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
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.84 | 0.97 | 40 | MG, POP, BTM |
| 2 | 139 | 0.67 | 0.88 | 30 | empty |
| 3 | 98 | 0.36 | 0.74 | 17 | 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 6AXM · PDBe 6AXM · UniProt Q9K499
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