Research workbench
2.25 ångström structure of the extracellular solute-binding protein from staphylococcus aureus in complex with maltose.
Analyse 2.25 ångström structure of the extracellular solute-binding protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HW8
- Type
- protein
- Length
- 752 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial extracellular solute-binding protein, putative
- UniProt
- Q2G1E9
- Ligands
- GLC, K, SO4, CL
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bacterial extracellular solute-binding protein, putative | protein | 376 | 45% helix, 21% strand | Q2G1E9 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
- K · Potassium ion · metal · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 14 copies · chains A, B
- CL · Chloride ion · ion · 3 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 | 967 | 0.70 | 0.75 | 108 | GLC |
| 2 | 320 | 0.54 | 0.75 | 34 | K |
| 3 | 64 | 0.52 | 0.86 | 19 | empty |
| 4 | 110 | 0.49 | 0.81 | 31 | SO4 |
| 5 | 63 | 0.48 | 0.84 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1384 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4HW8 · 2.25 Angstrom Structure of the Extracellular Solute-binding Protein from Staphylococcus… · 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 Q2G1E9
- Elsewhere: RCSB PDB 4HW8 · PDBe 4HW8 · UniProt Q2G1E9
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