MolNFT v1 · #153431 · protein
Crystal structure of a beta-N-acetylhexosaminidase
6JE8: “Crystal structure of a beta-N-acetylhexosaminidase”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.58). MolNFT v1 #153431 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6JE8
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-N-acetylhexosaminidase
- EC
- 3.2.1.52
- UniProt
- B2UP57
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-N-acetylhexosaminidase (EC 3.2.1.52) | protein | 469 | 36% helix, 19% strand | B2UP57 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · 5 copies · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.58 | 0.77 | 35 | GOL |
| 2 | 84 | 0.39 | 0.77 | 15 | empty |
| 3 | 74 | 0.34 | 0.75 | 16 | 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 B2UP57
- Elsewhere: RCSB PDB 6JE8 · PDBe 6JE8 · UniProt B2UP57
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