1uyq

mutated b-glucosidase A from Paenibacillus polymyxa showing increased stability

Method: X-RAY DIFFRACTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

BETA-GLUCOSIDASE A

PAENIBACILLUS POLYMYXA

UniProt P22073

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 8 2-deoxy-2-fluoro-alpha-D-glucopyranose × 8 2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-D-glucopyranoside × 8 water × 8 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BGLA_PAEPO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–447; UniProt 2–448

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1uyq
Deposition date deposition_date2004-03-02
Structure title titlemutated b-glucosidase A from Paenibacillus polymyxa showing increased stability
Keywords keywordsHYDROLASE, B-GLUCOSIDASE, MUTATION AFFECTING STABILITY, HYDROLASE GLYCOSIDASE, CELLULOSE DEGRADATION; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1uyq__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1uyq__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1uyq__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)48.79 Å
Rg (electron density)47.96 Å
Total Rg48.19 Å
Atom count29392
Residues3576
Excluded volume515680 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1uyq__assembly_1__model_1 octameric (8) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (4)

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1uyqa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.8 — (Trans)glycosidases
Family Family familyc.1.8.4 — Family 1 of glycosyl hydrolase

CATH v4.4 (1 domains)

Domain ID domain_id1uyqA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases

7. Citations (2)