4v44

E. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE

Method: X-RAY DIFFRACTION Dmax: 418.3 Å Quality: REASONABLE

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 Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1023 Chain B; UniProt 1–1023 Chain C; UniProt 1–1023 Chain D; UniProt 1–1023 Non-standard monomer:Yes (specific site not provided by mmCIF) 2-deoxy-2-fluoro-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 4 MG MAGNESIUM ION × 8 NA SODIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;295 K;Cacodylate, PEG 8000, MgSO4, NaCl, BME, pH 5.9, VAPOR DIFFUSION, HANGING DROP at 295K, pH 5.90 Resolution 2.70 Å
2 Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–1023 Chain F; UniProt 1–1023 Chain G; UniProt 1–1023 Chain H; UniProt 1–1023 Non-standard monomer:Yes (specific site not provided by mmCIF) 2-deoxy-2-fluoro-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 4 MG MAGNESIUM ION × 8 NA SODIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;295 K;Cacodylate, PEG 8000, MgSO4, NaCl, BME, pH 5.9, VAPOR DIFFUSION, HANGING DROP at 295K, pH 5.90 Resolution 2.70 Å
3 Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 1–1023 Chain J; UniProt 1–1023 Chain K; UniProt 1–1023 Chain L; UniProt 1–1023 Non-standard monomer:Yes (specific site not provided by mmCIF) 2-deoxy-2-fluoro-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 4 MG MAGNESIUM ION × 8 NA SODIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;295 K;Cacodylate, PEG 8000, MgSO4, NaCl, BME, pH 5.9, VAPOR DIFFUSION, HANGING DROP at 295K, pH 5.90 Resolution 2.70 Å
4 Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 1–1023 Chain N; UniProt 1–1023 Chain O; UniProt 1–1023 Chain P; UniProt 1–1023 Non-standard monomer:Yes (specific site not provided by mmCIF) 2-deoxy-2-fluoro-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 4 MG MAGNESIUM ION × 8 NA SODIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;295 K;Cacodylate, PEG 8000, MgSO4, NaCl, BME, pH 5.9, VAPOR DIFFUSION, HANGING DROP at 295K, pH 5.90 Resolution 2.70 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 80 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 1–1023; UniProt 1–1023 Author chain B; PDBConstruct 1–1023; UniProt 1–1023 Author chain C; PDBConstruct 1–1023; UniProt 1–1023 Author chain D; PDBConstruct 1–1023; UniProt 1–1023 Author chain E; PDBConstruct 1–1023; UniProt 1–1023 Author chain F; PDBConstruct 1–1023; UniProt 1–1023 Author chain G; PDBConstruct 1–1023; UniProt 1–1023 Author chain H; PDBConstruct 1–1023; UniProt 1–1023 Author chain I; PDBConstruct 1–1023; UniProt 1–1023 Author chain J; PDBConstruct 1–1023; UniProt 1–1023 Author chain K; PDBConstruct 1–1023; UniProt 1–1023 Author chain L; PDBConstruct 1–1023; UniProt 1–1023 Author chain M; PDBConstruct 1–1023; UniProt 1–1023 Author chain N; PDBConstruct 1–1023; UniProt 1–1023 Author chain O; PDBConstruct 1–1023; UniProt 1–1023 Author chain P; PDBConstruct 1–1023; UniProt 1–1023

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 4v44

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v44
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v44
Deposition date deposition_date2001-09-13
Structure title titleE. COLI (lacZ) BETA-GALACTOSIDASE IN COMPLEX WITH 2-F-LACTOSE
Keywords keywordsTIM BARREL (ALPHA/BETA BARREL), JELLY-ROLL BARREL, IMMUNOGLOBULIN, BETA SUPERSANDWICH, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron152.30
Forward intensity I(0) i049927100000.00
Molecular weight molecular_weight1867700.0 kDa
Excluded volume excluded_volume2314100 ų
Envelope volume envelope_volume3949000 ų
Hydration-shell volume shell_volume250200 ų
Envelope diameter envelope_diameter546.9
Shell Rg shell_rg95.41
Envelope Rg envelope_rg151.40
Shape Rg shape_rg152.30
Total Rg total_rg152.10
Total atoms total_atoms131792
Residues n_residues16288
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 dmax418.3
Rg (real space) rg_real137.30
Rg uncertainty (real space) rg_real_error3.04
I(0) (real space) i0_real4.7670e+10
I(0) uncertainty (real space) i0_real_error1.3170e+09
Rg (reciprocal space) rg_reciprocal106.90
I(0) (reciprocal space) i0_reciprocal43610000000.0000
Solution quality estimate total_estimate0.6197
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.7
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.799
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha0.8713
Highest regularization parameter α highest_alpha420900000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.061; Oscil: 0.794; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.012

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (5)

9. Files and Curves (10)