Research workbench
Saccharomyces cerevisiae lanosterol 14-alpha demethylase with lanosterol bound
Analyse Saccharomyces cerevisiae lanosterol 14-alpha demethylase with lanosterol bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LXJ
- Type
- protein
- Length
- 530 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lanosterol 14-alpha demethylase
- EC
- 1.14.13.70
- UniProt
- P10614
- Ligands
- HEM, LAN, OXY
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lanosterol 14-alpha demethylase (EC 1.14.13.70) | protein | 530 | 52% helix, 10% strand | P10614 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- LAN · Lanosterol · ligand · chains A
- OXY · Oxygen molecule · ion · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 798 | 0.87 | 0.89 | 74 | HEM, LAN, OXY |
| 2 | 300 | 0.60 | 0.78 | 38 | empty |
| 3 | 198 | 0.55 | 0.79 | 39 | empty |
| 4 | 127 | 0.46 | 0.77 | 21 | empty |
Compared structures
- 4LXJ · Saccharomyces cerevisiae lanosterol 14-alpha demethylase with lanosterol bound · the same entry in another collection · chain A against A, TM-score 1.00
- P10614 · AlphaFold monomer V2.0 prediction for lanosterol 14-alpha demethylase (P10614) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P10614
- Elsewhere: RCSB PDB 4LXJ · PDBe 4LXJ · UniProt P10614
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