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Crystal structure of neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides
Analyse Crystal structure of neisseria polysaccharea amylosucrase mutant efficient for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N7J
- 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
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylosucrase (EC 2.4.1.4) | protein | 628 | 43% helix, 15% strand | Q9ZEU2 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A
- FRU · beta-D-fructofuranose · sugar · 3 copies · chains A
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- PG4 · Tetraethylene glycol · 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 | 533 | 0.80 | 0.86 | 63 | TRS |
| 2 | 205 | 0.60 | 0.81 | 35 | empty |
| 3 | 70 | 0.44 | 0.82 | 14 | empty |
| 4 | 53 | 0.25 | 0.72 | 15 | 1PE |
Compared structures
- 5N7J · Crystal structure of Neisseria polysaccharea amylosucrase mutant efficient for the… · 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 5N7J · PDBe 5N7J · UniProt Q9ZEU2
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