MolNFT v1 · #59319 · protein
Bace-1 complexed with compound 3
3BUG · Beta-secretase 1: “Bace-1 complexed with compound 3”. X-ray diffraction, 1 ligand (AEH), 1 pocket (best druggability 0.65). MolNFT v1 #59319 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3BUG
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-secretase 1
- EC
- 3.4.23.46
- UniProt
- P56817
- Ligands
- AEH
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-secretase 1 (EC 3.4.23.46) | protein | 357 | 16% helix, 42% strand | P56817 |
Ligands and binding sites
- AEH · 4-(2-aminoethyl)-2-ethylphenol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.65 | 0.78 | 56 | AEH |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P56817
- Elsewhere: RCSB PDB 3BUG · PDBe 3BUG · UniProt P56817
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