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UniProt Q42975

Beta-glucosidase (Q42975)

Beta-glucosidase (UniProt Q42975), EC 3.2.1.21: 12 experimental structures on GenesisL1, 4 ligands bound, 30 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q42975
Protein
Beta-glucosidase
EC
3.2.1.21
Experimental structures
12
Predicted models
0
Ligands
4
Pockets
30 · 6 records with a druggable one

Structures

12 records of Q42975 in the MolNFT archive: 12 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2RGLRice BGlu1 beta-glucosidase, a plant exoglucanase/beta-glucosidasex-ray diffractionA, BZN, SO46 (best 0.70)
2RGLRice BGLU1 beta-glucosidase, a plant EXOGLUCANASE/BETA-glucosidasex-ray diffractionA, B——
2RGMRice BGlu1 beta-glucosidase, a plant exoglucanase/beta-glucosidasex-ray diffractionA, BG2F, ZN, SO46 (best 0.68)
2RGMRice BGLU1 beta-glucosidase, a plant EXOGLUCANASE/BETA-glucosidasex-ray diffractionA, B——
3F4VSemi-active E176Q mutant of rice BGlu1, a plant exoglucanase/beta-glucosidasex-ray diffractionA, BZN, SO44 (best 0.68)
3F4VSemi-active E176Q mutant of rice BGLU1, a plant EXOGLUCANASE/BETA- glucosidasex-ray diffractionA, B——
3F5JSemi-active E176Q mutant of rice BGlu1, a plant exoglucanase/beta-glucosidasex-ray diffractionA, BBGC, ZN, SO44 (best 0.68)
3F5JSemi-active E176Q mutant of rice BGLU1, a plant EXOGLUCANASE/BETA- glucosidasex-ray diffractionA, B——
3F5KSemi-active E176Q mutant of rice BGlu1, a plant exoglucanase/beta-glucosidasex-ray diffractionA, BBGC, ZN, SO45 (best 0.68)
3F5KSemi-active E176Q mutant of rice BGLU1, a plant EXOGLUCANASE/BETA- glucosidasex-ray diffractionA, B——
3F5LSemi-active E176Q mutant of rice BGlu1, a plant exoglucanase/beta-glucosidasex-ray diffractionA, BBGC, ZN, SO45 (best 0.68)
3F5LSemi-active E176Q mutant of rice BGLU1, a plant EXOGLUCANASE/BETA- glucosidasex-ray diffractionA, B——

Ligands

  • SO4 · Sulfate ion · in 6 records
  • ZN · Zinc ion · in 6 records
  • BGC · beta-D-glucopyranose · in 3 records
  • G2F · 2-deoxy-2-fluoro-alpha-D-glucopyranose · in 1 record

Elsewhere

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