Research workbench
Structure of human osc in complex with lanosterol
Analyse Structure of human osc in complex with lanosterol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W6K
- Type
- protein
- Length
- 725 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lanosterol synthase
- EC
- 5.4.99.7
- UniProt
- P48449
- Ligands
- LAN
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lanosterol synthase (EC 5.4.99.7) | protein | 725 | 51% helix, 6% strand | P48449 |
Ligands and binding sites
- LAN · Lanosterol · ligand · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.85 | 0.96 | 35 | LAN |
| 2 | 219 | 0.77 | 0.91 | 23 | BOG |
| 3 | 311 | 0.62 | 0.79 | 25 | empty |
| 4 | 171 | 0.60 | 0.83 | 35 | empty |
| 5 | 122 | 0.46 | 0.78 | 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 P48449
- Elsewhere: RCSB PDB 1W6K · PDBe 1W6K · UniProt P48449
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