Research workbench
Saccharomyces cerevisiae CYP51 complexed with the plant pathogen inhibitor fluquinconazole
Analyse Saccharomyces cerevisiae CYP51 complexed with the plant pathogen inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EAF
- Type
- protein
- Length
- 1,056 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lanosterol 14-alpha demethylase
- UniProt
- A6ZSR0
- Ligands
- HEM, FQC
- Pockets
- 13 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lanosterol 14-alpha demethylase | protein | 528 | 52% helix, 11% strand | A6ZSR0 |
| B | Lanosterol 14-alpha demethylase | protein | 528 | 51% helix, 11% strand | A6ZSR0 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- FQC · 3-(2,4-dichlorophenyl)-6-fluoranyl-2-(1,2,4-triazol-1-yl)quinazolin-4-one · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 822 | 0.87 | 0.89 | 72 | HEM, FQC |
| 2 | 832 | 0.87 | 0.89 | 75 | HEM, FQC |
| 3 | 515 | 0.71 | 0.80 | 48 | empty |
| 4 | 273 | 0.61 | 0.79 | 34 | empty |
| 5 | 271 | 0.60 | 0.79 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 586 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5EAF · Saccharomyces cerevisiae CYP51 complexed with the plant pathogen inhibitor Fluquinconazole · 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 A6ZSR0
- Elsewhere: RCSB PDB 5EAF · PDBe 5EAF · UniProt A6ZSR0
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