MolNFT v1 · #118047 · protein
Crystal structure of lanosterol 14-alpha demethylase with intact transmembrane domain bound to itraconazole
5EQB: “Crystal structure of lanosterol 14-alpha demethylase with intact transmembrane domain bound to itraconazole”. X-ray diffraction, 2 ligands (HEM, 1YN), 5 pockets (best druggability 0.87). MolNFT v1 #118047 on GenesisL1: 3D structure…
- PDB
- 5EQB
- Type
- protein
- Length
- 531 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, 1YN
- Pockets
- 5 · 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 | 531 | 52% helix, 10% strand | P10614 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- 1YN · 2-[(2R)-butan-2-yl]-4-{4-[4-(4-{[(2R,4S)-2-(2,4-dichlorophenyl)-2-(1H-1,2,4-triazol-1-ylmethyl)-1,3-dioxolan-4-yl]methoxy}phenyl)piperazin-1-yl]phenyl}-2,4-dihydro-3H-1,2,4-triazol-3-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 882 | 0.87 | 0.89 | 75 | HEM, 1YN |
| 2 | 268 | 0.60 | 0.78 | 33 | empty |
| 3 | 181 | 0.58 | 0.81 | 37 | empty |
| 4 | 132 | 0.45 | 0.77 | 24 | empty |
| 5 | 52 | 0.28 | 0.76 | 11 | empty |
Compared structures
- 5EQB · Crystal structure of lanosterol 14-alpha demethylase with intact transmembrane domain… · 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 0.98
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 5EQB · PDBe 5EQB · UniProt P10614
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