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Crystal structure of ruminiclostridium thermocellum beta-glucosidase a

Analyse Crystal structure of ruminiclostridium thermocellum beta-glucosidase a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OGZ
Type
protein
Length
898 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-glucosidase a
EC
3.2.1.21
UniProt
P26208
Ligands
SO4
Pockets
6 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta-glucosidase a (EC 3.2.1.21)protein44944% helix, 17% strandP26208

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13240.730.8543empty
26510.720.7956empty
36280.720.7960empty
4620.410.8016empty
5940.340.7420empty

Interfaces

1 interface between chains.

  • A–B · 615 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 5OGZ · Crystal structure of Ruminiclostridium Thermocellum beta-Glucosidase A · the same entry in another collection · chain A against A, TM-score 1.00
  • P26208 · AlphaFold monomer V2.0 prediction for beta-glucosidase a (P26208) · a predicted model of the same protein · chain A against A, TM-score 0.99

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