8ri6

Beta-galactosidase (LacZ) purified from E. coli.

Method: ELECTRON MICROSCOPY Dmax: 177.9 Å Quality: GOOD

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

Beta-galactosidase

Escherichia coli

UniProt P00722

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1024 Chain B; UniProt 1–1024 Chain C; UniProt 1–1024 Chain D; UniProt 1–1024 Not recorded MG MAGNESIUM ION × 8 NA SODIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM Tris, 50 mM NaCl, 2 mM MgCl2, 2 mM EDTA, 1 mM TCEP, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.06 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

67 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BGAL_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1024; UniProt 1–1024 Author chain B; PDBConstruct 1–1024; UniProt 1–1024 Author chain C; PDBConstruct 1–1024; UniProt 1–1024 Author chain D; PDBConstruct 1–1024; UniProt 1–1024

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8ri6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ri6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ri6
Deposition date deposition_date2023-12-18
Structure title titleBeta-galactosidase (LacZ) purified from E. coli.
Keywords keywordsbeta-galactosidase, inhibitor, iminosugar, plant pathogenic bacteria., HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier52.47
Radius of gyration Rg (electron density) rg_electron52.13
Forward intensity I(0) i03171980000.00
Molecular weight molecular_weight462530.0 kDa
Excluded volume excluded_volume573310 ų
Envelope volume envelope_volume760590 ų
Hydration-shell volume shell_volume116740 ų
Envelope diameter envelope_diameter185.4
Shell Rg shell_rg59.48
Envelope Rg envelope_rg51.32
Shape Rg shape_rg52.11
Total Rg total_rg52.40
Total atoms total_atoms32652
Residues n_residues4064
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax177.9
Rg (real space) rg_real52.36
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real3.1720e+09
I(0) uncertainty (real space) i0_real_error6.0680e+07
Rg (reciprocal space) rg_reciprocal52.54
I(0) (reciprocal space) i0_reciprocal3173000000.0000
Solution quality estimate total_estimate0.8691
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.2
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.219
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha579000000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)