MolNFT v1 · #4900 · protein
Crystal structure of an arylsulfatase a mutant C69S
1E1Z: “Crystal structure of an arylsulfatase a mutant C69S”. X-ray diffraction, 2 ligands (NAG, MG), 1 pocket (best druggability 0.43). MolNFT v1 #4900 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1E1Z
- 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
- NAG, MG
- Pockets
- 1 · best druggability 0.43
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
- 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 | 132 | 0.43 | 0.76 | 25 | empty |
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 1E1Z · PDBe 1E1Z · UniProt P15289
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