Research workbench
Thermus thermophilus GLUCOSE/GALACTOSE binding protein bound with galactose
Analyse Thermus thermophilus GLUCOSE/GALACTOSE binding protein bound with galactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B3F
- Type
- protein
- Length
- 2,351 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-binding protein
- UniProt
- Q72KX2
- Ligands
- GAL
- Pockets
- 14 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F | Glucose-binding protein | protein | 392 | 53% helix, 15% strand | Q72KX2 |
| C | Glucose-binding protein | protein | 391 | 53% helix, 15% strand | Q72KX2 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 680 | 0.82 | 0.86 | 99 | empty |
| 2 | 1131 | 0.81 | 0.82 | 106 | empty |
| 3 | 433 | 0.78 | 0.87 | 45 | empty |
| 4 | 781 | 0.77 | 0.81 | 103 | empty |
| 5 | 1162 | 0.75 | 0.78 | 88 | empty |
Interfaces
8 interfaces between chains.
- E–F · 1036 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 987 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 802 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 543 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 328 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2B3F · Thermus thermophilus Glucose/Galactose Binding Protein Bound With Galactose · 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 Q72KX2
- Elsewhere: RCSB PDB 2B3F · PDBe 2B3F · UniProt Q72KX2
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