4v41

E. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC)

Method: X-RAY DIFFRACTION Dmax: 414.9 Å Quality: GOOD

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

BETA-GALACTOSIDASE

OrganismNot specified

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 1–1023 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) MG MAGNESIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;293 K;PEG 8000, Cacodylate, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 2.50 Å R-free 0.207
2 Protein homooligomer Homooligomer Protein × 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) MG MAGNESIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;293 K;PEG 8000, Cacodylate, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 2.50 Å R-free 0.207
3 Protein homooligomer Homooligomer Protein × 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) MG MAGNESIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;293 K;PEG 8000, Cacodylate, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 2.50 Å R-free 0.207
4 Protein homooligomer Homooligomer Protein × 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) MG MAGNESIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.9;293 K;PEG 8000, Cacodylate, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 20K Resolution 2.50 Å R-free 0.207

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 4v41

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v41
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v41
Deposition date deposition_date2000-06-07
Structure title titleE. COLI (LAC Z) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-MONOCLINIC)
Keywords keywordsalpha/beta barrel, jelly roll barrel, fibronectin, 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_electron152.40
Forward intensity I(0) i049688100000.00
Molecular weight molecular_weight1861500.0 kDa
Excluded volume excluded_volume2305900 ų
Envelope volume envelope_volume3930800 ų
Hydration-shell volume shell_volume250140 ų
Envelope diameter envelope_diameter543.9
Shell Rg shell_rg95.23
Envelope Rg envelope_rg150.70
Shape Rg shape_rg152.40
Total Rg total_rg152.20
Total atoms total_atoms131392
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 dmax414.9
Rg (real space) rg_real136.80
Rg uncertainty (real space) rg_real_error2.96
I(0) (real space) i0_real4.7380e+10
I(0) uncertainty (real space) i0_real_error1.2220e+09
Rg (reciprocal space) rg_reciprocal107.00
I(0) (reciprocal space) i0_reciprocal43400000000.0000
Solution quality estimate total_estimate0.8497
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.0
Skewness Skewness skewness0.465
Kurtosis Kurtosis kurtosis-0.808
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha0.7354
Highest regularization parameter α highest_alpha427800000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.065; Oscil: 0.803; Stabil: 0.982; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 0.013

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (4)

9. Files and Curves (10)