Research workbench
Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656)
Analyse Crystal structure of recombinant human beta-glucocerebrosidase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q6L
- Type
- protein
- Length
- 992 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosylceramidase
- EC
- 3.2.1.45
- UniProt
- P04062
- Ligands
- RJR, NAG, BMA, SO4
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosylceramidase (EC 3.2.1.45) | protein | 497 | 28% helix, 28% strand | P04062 |
| B | Glucosylceramidase (EC 3.2.1.45) | protein | 495 | 27% helix, 29% strand | P04062 |
Ligands and binding sites
- RJR · (1~{S},2~{R},3~{R},4~{S},5~{S})-4-[[4-[3-(1-adamantylmethoxy)propyl]-1,2,3-triazol-1-yl]methyl]cyclohexane-1,2,3,5-tetrol · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar
- SO4 · Sulfate ion · ion · 19 copies · chains A, B
- ACT · Acetate ion · additive · 24 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 851 | 0.82 | 0.84 | 84 | ACT, SO4, RJR |
| 2 | 211 | 0.56 | 0.79 | 41 | empty |
| 3 | 77 | 0.41 | 0.79 | 23 | SO4 |
| 4 | 69 | 0.35 | 0.77 | 18 | ACT |
| 5 | 60 | 0.32 | 0.77 | 19 | ACT |
Interfaces
1 interface between chains.
- A–B · 640 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 3 glycan, 2 covalent (disulfide, N-glycosylation, covalent ligand).
Compared structures
- 6Q6L · Crystal structure of recombinant human beta-glucocerebrosidase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P04062 · AlphaFold monomer V2.0 prediction for lysosomal acid glucosylceramidase (P04062) · a predicted model of the same protein · chain B 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 P04062
- Elsewhere: RCSB PDB 6Q6L · PDBe 6Q6L · UniProt P04062
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.