Research workbench
Human arylsulfatase a
Analyse Human arylsulfatase a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AUK
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Homo sapiens
- Molecule
- Arylsulfatase a
- EC
- 3.1.6.8
- UniProt
- P15289
- Ligands
- NAG, MG
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 30% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arylsulfatase a (EC 3.1.6.8) | protein | 481 | 30% helix, 19% strand | P15289 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.43 | 0.77 | 28 | MG |
| 2 | 60 | 0.37 | 0.79 | 18 | empty |
Modifications
Observed in the structure: 6 disulfide, 1 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 P15289
- Elsewhere: RCSB PDB 1AUK · PDBe 1AUK · UniProt P15289
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