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X-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic bacterium alicyclobacillus acidocaldarius

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
1URS
Type
protein
Length
731 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 0.67

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMaltose-binding proteinprotein36645% helix, 20% strandQ9RHZ6
BMaltose-binding proteinprotein36545% helix, 19% strandQ9RHZ6

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, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13450.670.8142GLC
23280.660.8137GLC
33040.640.8035empty
41310.530.8124empty
51960.520.7729empty

Interfaces

1 interface between chains.

  • A–B · 486 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 1URS · 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

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