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Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA

Analyse Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2G3M
Type
protein
Length
4,147 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.55
Source
Sulfolobus solfataricus
Molecule
Alpha-glucosidase
EC
3.2.1.20
UniProt
O59645
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · resolution 2.55 · 2 distinct chains · 25% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EAlpha-glucosidase (EC 3.2.1.20)protein69126% helix, 31% strandO59645
FAlpha-glucosidase (EC 3.2.1.20)protein69225% helix, 30% strandO59645

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111880.860.87144empty
26800.820.8682empty
36080.820.8776empty
45730.810.8776empty
54640.800.8868empty

Interfaces

12 interfaces between chains.

  • E–F · 1605 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 1579 Ų buried · 24 hydrogen bonds · protein-protein
  • D–E · 1563 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 1549 Ų buried · 23 hydrogen bonds · protein-protein
  • D–F · 1541 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 2G3M · Crystal structure of the sulfolobus solfataricus alpha- glucosidase mala · the same entry in another collection · chain A against A, TM-score 1.00

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