Research workbench
Crystal structure of sugar transporter BL01359 from bacillus licheniformis, target efi-510856, in complex with stachyose
Analyse Crystal structure of sugar transporter BL01359 from bacillus licheniformis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RK9
- Type
- protein
- Length
- 768 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbohydrate ABC transporter substrate-binding protein msme
- UniProt
- Q65LL6
- Ligands
- GLA, GLC, FRU
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbohydrate ABC transporter substrate-binding protein msme | protein | 384 | 46% helix, 15% strand | Q65LL6 |
Ligands and binding sites
- GLA · alpha-D-galactopyranose · sugar · 4 copies · chains A, B
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.85 | 0.86 | 106 | GLC, GLA, FRU |
| 2 | 204 | 0.57 | 0.80 | 38 | empty |
| 3 | 177 | 0.52 | 0.78 | 34 | empty |
| 4 | 85 | 0.41 | 0.78 | 20 | empty |
| 5 | 121 | 0.38 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 608 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4RK9 · CRYSTAL STRUCTURE OF SUGAR TRANSPORTER BL01359 FROM Bacillus licheniformis, TARGET… · 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 Q65LL6
- Elsewhere: RCSB PDB 4RK9 · PDBe 4RK9 · UniProt Q65LL6
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