MolNFT v2 · #1206 · protein

Human arylsulfatase a

1AUK: “Human arylsulfatase a”. X-ray diffraction at 2.1, 2 ligands (NAG, MG), 2 pockets (best druggability 0.43). MolNFT v2 #1206 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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.

Pocket	Volume (Å³)	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

1AUK · 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 1AUK · PDBe 1AUK · UniProt P15289

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