Research workbench
Crystal structure of the active site mutant GLU328GLN of amylosucrase from neisseria polysaccharea in complex with the natural substrate sucrose
Analyse Crystal structure of the active site mutant GLU328GLN of amylosucrase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JGI
- 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
- 6 · best druggability 0.75
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
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 | 404 | 0.75 | 0.85 | 51 | GLC, FRU |
| 2 | 192 | 0.58 | 0.80 | 36 | empty |
| 3 | 72 | 0.42 | 0.80 | 13 | empty |
| 4 | 55 | 0.32 | 0.77 | 13 | empty |
| 5 | 65 | 0.30 | 0.74 | 18 | empty |
Compared structures
- 1JGI · Crystal Structure of the Active Site Mutant Glu328Gln of Amylosucrase 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 1JGI · PDBe 1JGI · UniProt Q9ZEU2
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