7zcd

Mutant L39Y-L58F of recombinant bovine beta-lactoglobulin in complex with pramocaine

Method: X-RAY DIFFRACTION Dmax: 51.1 Å Quality: GOOD

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

Beta-lactoglobulin

Bos taurus

UniProt P02754

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain AAA; UniProt 19–178 Mutation:L1A, I2S, L39Y, L58F PX9 Pramocaine × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;2.2M ammonium sulfate, 0.5 M Tris-HCl, pH 8.5 Resolution 2.10 Å R-free 0.269

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.

101 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LACB_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 3–162; UniProt 19–178

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 7zcd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zcd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zcd
Deposition date deposition_date2022-03-27
Structure title titleMutant L39Y-L58F of recombinant bovine beta-lactoglobulin in complex with pramocaine
Keywords keywordslactoglobulin, mutation, ligand, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.07
Radius of gyration Rg (electron density) rg_electron14.57
Forward intensity I(0) i05748330.00
Molecular weight molecular_weight17755.0 kDa
Excluded volume excluded_volume22488 ų
Envelope volume envelope_volume25077 ų
Hydration-shell volume shell_volume14229 ų
Envelope diameter envelope_diameter49.3
Shell Rg shell_rg20.75
Envelope Rg envelope_rg14.95
Shape Rg shape_rg14.56
Total Rg total_rg15.86
Total atoms total_atoms1243
Residues n_residues153
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 dmax51.1
Rg (real space) rg_real15.93
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real5.7480e+06
I(0) uncertainty (real space) i0_real_error5.7420e+04
Rg (reciprocal space) rg_reciprocal15.95
I(0) (reciprocal space) i0_reciprocal5748000.0000
Solution quality estimate total_estimate0.8869
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.031
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1513000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)