MolNFT v2 · #4944 · protein
Crystal structure of an Arylsulfatase A mutant P426L
1E33: “Crystal structure of an Arylsulfatase A mutant P426L”. X-ray diffraction at 2.5, 2 ligands (NAG, MG), 1 pocket (best druggability 0.40). MolNFT v2 #4944 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1E33
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Homo sapiens
- Molecule
- Arylsulfatase A
- EC
- 3.1.6.8
- UniProt
- P15289
- Ligands
- NAG, MG
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · resolution 2.5 · 1 distinct chain · 28% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Arylsulfatase A (EC 3.1.6.8) | protein | 481 | 28% helix, 20% strand | P15289 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains P
- MG · Magnesium ion · metal · chains P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.40 | 0.76 | 24 | 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 1E33 · PDBe 1E33 · UniProt P15289
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