Research workbench
Alpha-glucan binding by a streptococcal virulence factor
Analyse Alpha-glucan binding by a streptococcal virulence factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J44
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline amylopullulanase
- UniProt
- Q97SQ7
- Ligands
- GLC, ZN
- Pockets
- 3 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkaline amylopullulanase | protein | 217 | 3% helix, 39% strand | Q97SQ7 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 7 copies · chains A
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.32 | 0.75 | 13 | empty |
| 2 | 71 | 0.31 | 0.74 | 14 | empty |
| 3 | 61 | 0.27 | 0.73 | 19 | empty |
Compared structures
- 2J44 · Alpha-glucan binding by a streptococcal virulence factor · 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
- Every structure of UniProt Q97SQ7
- Elsewhere: RCSB PDB 2J44 · PDBe 2J44 · UniProt Q97SQ7
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