MolNFT v1 · #4927 · protein
Crystal structure of an arylsulfatase a mutant C69A
1E2S: “Crystal structure of an arylsulfatase a mutant C69A”. X-ray diffraction, 3 ligands (CSN, NAG, MG), 2 pockets (best druggability 0.78). MolNFT v1 #4927 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1E2S
- Type
- protein
- Length
- 481 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
- CSN, NAG, MG
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Arylsulfatase a (EC 3.1.6.8) | protein | 481 | 29% helix, 19% strand | P15289 |
Ligands and binding sites
- CSN · N,4-dihydroxy-N-oxo-3-(sulfooxy)benzenaminium · ligand · chains P
- 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.78 | 0.99 | 20 | empty |
| 2 | 134 | 0.43 | 0.76 | 27 | CSN |
Modifications
Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).
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 1E2S · PDBe 1E2S · UniProt P15289
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