Research workbench
Crystal structure of 4-sulfatase (human)
Analyse Crystal structure of 4-sulfatase (human) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FSU
- Type
- protein
- Length
- 475 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylgalactosamine-4-sulfatase
- EC
- 3.1.6.12
- UniProt
- P15848
- Ligands
- NAG, CA, CL
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylgalactosamine-4-sulfatase (EC 3.1.6.12) | protein | 475 | 28% helix, 18% strand | P15848 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.41 | 0.76 | 24 | empty |
| 2 | 78 | 0.38 | 0.77 | 16 | empty |
| 3 | 66 | 0.35 | 0.77 | 21 | empty |
Modifications
Observed in the structure: 4 disulfide, 2 glycan, 1 modified (disulfide, N-glycosylation, nonstandard).
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 P15848
- Elsewhere: RCSB PDB 1FSU · PDBe 1FSU · UniProt P15848
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.