Research workbench
Crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Analyse Crystal structure of a covalent intermediate of endogenous 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
- 1N2K
- Type
- protein
- Length
- 482 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arylsulfatase a
- EC
- 3.1.6.8
- UniProt
- P15289
- Ligands
- NAG, CA
- Pockets
- 3 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arylsulfatase a (EC 3.1.6.8) | protein | 482 | 27% helix, 18% strand | P15289 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- CA · Calcium ion · metal · 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 | 56 | 0.37 | 0.79 | 19 | empty |
| 2 | 101 | 0.35 | 0.74 | 23 | empty |
| 3 | 60 | 0.29 | 0.74 | 20 | empty |
Modifications
Observed in the structure: 6 disulfide, 2 glycan, 1 modified (disulfide, N-glycosylation, nonstandard).
Compared structures
- 1N2K · Crystal structure of a covalent intermediate of endogenous human arylsulfatase A · the same entry in another collection · chain A against A, TM-score 1.00
- P15289 · AlphaFold monomer V2.0 prediction for arylsulfatase a (P15289) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 1N2K · PDBe 1N2K · UniProt P15289
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.