4ckd

Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.

Method: ELECTRON MICROSCOPY Dmax: 180.3 Å Quality: GOOD

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

BETA-GALACTOSIDASE

ESCHERICHIA COLI K-12

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) 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 SCFV13R4 ANTIBODY FV HEAVY CHAIN × 4 SCFV13R4 ANTIBODY FV LIGHT CHAIN × 4 ELECTRON MICROSCOPY cryo-EM buffer:20% PHOSPHATE BUFFERED SALINE (PBS);pH 7.4;20% PHOSPHATE BUFFERED SALINE (PBS) cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 100, INSTRUMENT- OTHER, METHOD- BLOT FOR 10-20 SECONDS UNTIL DIAMETER OF BLOTTED MENISCUS CEASES TO EXPAND, BEFORE PLUNGING. Resolution 13.00 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 4ckd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ckd
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4ckd
Deposition date deposition_date2014-01-03
Structure title titleModel of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.
Keywords keywordsHYDROLASE-IMMUNE SYSTEM COMPLEX; HYDROLASE/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.98
Radius of gyration Rg (electron density) rg_electron55.58
Forward intensity I(0) i04657390000.00
Molecular weight molecular_weight561850.0 kDa
Excluded volume excluded_volume696070 ų
Envelope volume envelope_volume920180 ų
Hydration-shell volume shell_volume131270 ų
Envelope diameter envelope_diameter184.1
Shell Rg shell_rg63.08
Envelope Rg envelope_rg54.81
Shape Rg shape_rg55.54
Total Rg total_rg55.87
Total atoms total_atoms39672
Residues n_residues4968
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 dmax180.3
Rg (real space) rg_real55.74
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real4.6570e+09
I(0) uncertainty (real space) i0_real_error9.2840e+07
Rg (reciprocal space) rg_reciprocal56.16
I(0) (reciprocal space) i0_reciprocal4660000000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.3
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.511
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha4278000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.816

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)