Research workbench
Crystal structure of amylosucrase inactive double mutant F290K-E328Q from neisseria polysaccharea in complex with sucrose.
Analyse Crystal structure of amylosucrase inactive double mutant F290K-E328Q from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FLS
- 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
- GLC, FRU, CL
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylosucrase (EC 2.4.1.4) | protein | 628 | 42% helix, 15% strand | Q9ZEU2 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.76 | 0.85 | 61 | GLC, FRU, CL |
| 2 | 173 | 0.58 | 0.81 | 35 | empty |
| 3 | 52 | 0.39 | 0.81 | 13 | empty |
| 4 | 59 | 0.27 | 0.73 | 12 | empty |
Compared structures
- 4FLS · Crystal structure of Amylosucrase inactive double mutant F290K-E328Q from Neisseria… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ZEU2 · AlphaFold monomer V2.0 prediction for amylosucrase (Q9ZEU2) · 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 Q9ZEU2
- Elsewhere: RCSB PDB 4FLS · PDBe 4FLS · UniProt Q9ZEU2
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