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Structure of human osc in complex with ro 48-8071
Analyse Structure of human osc in complex with ro 48-8071 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W6J
- Type
- protein
- Length
- 727 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
- R71, C14
- Pockets
- 8 · best druggability 0.84
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 | 727 | 51% helix, 6% strand | P48449 |
Ligands and binding sites
- R71 · [4-({6-[allyl(methyl)amino]hexyl}oxy)-2-fluorophenyl](4-bromophenyl)methanone · ligand · chains A
- C14 · Tetradecane · ligand · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.84 | 0.96 | 36 | R71 |
| 2 | 159 | 0.71 | 0.89 | 22 | C14 |
| 3 | 52 | 0.70 | 0.98 | 15 | empty |
| 4 | 329 | 0.63 | 0.79 | 27 | empty |
| 5 | 186 | 0.60 | 0.82 | 36 | 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 1W6J · PDBe 1W6J · UniProt P48449
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