4v40

BETA-GALACTOSIDASE

Method: X-RAY DIFFRACTION Dmax: 441.2 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 Not recorded MG MAGNESIUM ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å
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 Not recorded MG MAGNESIUM ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å
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 Not recorded MG MAGNESIUM ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å
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 Not recorded MG MAGNESIUM ION × 7 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 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 4v40

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v40
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4v40
Deposition date deposition_date1994-07-18
Structure title titleBETA-GALACTOSIDASE
Keywords keywordsHYDROLASE (O-GLYCOSYL); HYDROLASE (O-GLYCOSYL)
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) i049439100000.00
Molecular weight molecular_weight1857800.0 kDa
Excluded volume excluded_volume2301700 ų
Envelope volume envelope_volume3978100 ų
Hydration-shell volume shell_volume252840 ų
Envelope diameter envelope_diameter547.3
Shell Rg shell_rg95.08
Envelope Rg envelope_rg150.90
Shape Rg shape_rg152.40
Total Rg total_rg152.20
Total atoms total_atoms131199
Residues n_residues16336
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 dmax441.2
Rg (real space) rg_real141.70
Rg uncertainty (real space) rg_real_error3.27
I(0) (real space) i0_real4.7780e+10
I(0) uncertainty (real space) i0_real_error1.2550e+09
Rg (reciprocal space) rg_reciprocal107.00
I(0) (reciprocal space) i0_reciprocal43180000000.0000
Solution quality estimate total_estimate0.8503
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary88.2
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.740
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha1.3240
Highest regularization parameter α highest_alpha417400000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.046; Oscil: 0.722; Stabil: 0.978; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.018

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)