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X-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic bacterium alicyclobacillus acidocaldarius provide insight into acid stability of proteins
Analyse X-ray structures of the maltose-maltodextrin binding protein of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1URD
- Type
- protein
- Length
- 739 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding protein
- UniProt
- Q9RHZ6
- Ligands
- GLC
- Pockets
- 7 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding protein | protein | 370 | 44% helix, 20% strand | Q9RHZ6 |
| B | Maltose-binding protein | protein | 369 | 45% helix, 19% strand | Q9RHZ6 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 662 | 0.71 | 0.78 | 69 | GLC |
| 2 | 438 | 0.67 | 0.79 | 42 | GLC |
| 3 | 351 | 0.62 | 0.78 | 40 | empty |
| 4 | 172 | 0.51 | 0.78 | 28 | empty |
| 5 | 159 | 0.48 | 0.77 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 411 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1URD · X-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic… · 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 Q9RHZ6
- Elsewhere: RCSB PDB 1URD · PDBe 1URD · UniProt Q9RHZ6
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