Research workbench
Covalent intermediate of the E328Q amylosucrase mutant
Analyse Covalent intermediate of the E328Q amylosucrase mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S46
- Type
- protein
- Length
- 628 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amylosucrase
- EC
- 2.4.1.4
- UniProt
- Q9ZEU2
- Ligands
- BGC
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylosucrase (EC 2.4.1.4) | protein | 628 | 41% helix, 16% strand | Q9ZEU2 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 433 | 0.75 | 0.85 | 64 | BGC |
| 2 | 184 | 0.60 | 0.82 | 32 | empty |
| 3 | 58 | 0.40 | 0.81 | 13 | empty |
| 4 | 51 | 0.32 | 0.77 | 14 | empty |
| 5 | 52 | 0.25 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 1 glycan (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 Q9ZEU2
- Elsewhere: RCSB PDB 1S46 · PDBe 1S46 · UniProt Q9ZEU2
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