MolNFT v1 · #66087 · protein
Human alpha-galactosidase catalytic mechanism 1. empty active site
3HG2 · Alpha-galactosidase a: “Human alpha-galactosidase catalytic mechanism 1. empty active site”. X-ray diffraction, 5 ligands (NAG, BMA, FUC), 3 pockets (best druggability 0.62). MolNFT v1 #66087 on GenesisL1: 3D structure, binding…
- PDB
- 3HG2
- Type
- protein
- Length
- 781 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-galactosidase a
- EC
- 3.2.1.22
- UniProt
- P06280
- Ligands
- NAG, BMA, FUC, GAL, SO4
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-galactosidase a (EC 3.2.1.22) | protein | 390 | 31% helix, 24% strand | P06280 |
| B | Alpha-galactosidase a (EC 3.2.1.22) | protein | 391 | 32% helix, 24% strand | P06280 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies
- FUC · alpha-L-fucopyranose · sugar
- GAL · beta-D-galactopyranose · sugar · chains B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- ACY · Acetic acid · additive · 3 copies · chains A, B
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 | 508 | 0.62 | 0.75 | 82 | ACY |
| 2 | 53 | 0.38 | 0.81 | 17 | empty |
| 3 | 61 | 0.34 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 998 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 6 glycan (disulfide, N-glycosylation).
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 P06280
- Elsewhere: RCSB PDB 3HG2 · PDBe 3HG2 · UniProt P06280
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.