Research workbench
Amylosucrase mutant E328Q in a ternary complex with sucrose and maltoheptaose
Analyse Amylosucrase mutant E328Q in a ternary complex with sucrose and maltoheptaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZS2
- 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
- Ligands
- GLC, FRU
- 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 | — |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A
- FRU · beta-D-fructofuranose · sugar · 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 | 440 | 0.76 | 0.85 | 54 | GLC, FRU |
| 2 | 202 | 0.59 | 0.81 | 34 | empty |
| 3 | 75 | 0.41 | 0.79 | 14 | empty |
| 4 | 94 | 0.39 | 0.76 | 23 | empty |
Compared structures
- 1ZS2 · Amylosucrase Mutant E328Q in a ternary complex with sucrose and maltoheptaose · the same entry in another collection · 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
- Elsewhere: RCSB PDB 1ZS2 · PDBe 1ZS2
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