7q2p

Beta-lactoglobulin mutant FAW (I56F/L39A/M107W) in complex with desipramine (FAW-DSM#2)

Method: X-RAY DIFFRACTION Dmax: 80.4 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 17–178 Chain BBB; UniProt 17–178 Mutation:L1A, I2S, L39A, I56F, M107W EDO 1,2-ETHANEDIOL × 2 DSM 3-(10,11-DIHYDRO-5H-DIBENZO[B,F]AZEPIN-5-YL)-N-METHYLPROPAN-1-AMINE × 3 SO4 SULFATE ION × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;2.40 M (NH4)2SO4, 0.5 M Tris-HCl pH 8.5 Resolution 1.69 Å R-free 0.235

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 1–162; UniProt 17–178 Author chain BBB; PDBConstruct 1–162; UniProt 17–178

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 7q2p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q2p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q2p
Deposition date deposition_date2021-10-25
Structure title titleBeta-lactoglobulin mutant FAW (I56F/L39A/M107W) in complex with desipramine (FAW-DSM#2)
Keywords keywordslactoglobulin, mutation, desipramine, 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_guinier22.08
Radius of gyration Rg (electron density) rg_electron21.44
Forward intensity I(0) i021017900.00
Molecular weight molecular_weight36046.0 kDa
Excluded volume excluded_volume45632 ų
Envelope volume envelope_volume53770 ų
Hydration-shell volume shell_volume21433 ų
Envelope diameter envelope_diameter79.5
Shell Rg shell_rg27.70
Envelope Rg envelope_rg21.80
Shape Rg shape_rg21.42
Total Rg total_rg22.34
Total atoms total_atoms2528
Residues n_residues308
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 dmax80.4
Rg (real space) rg_real22.13
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real2.1020e+07
I(0) uncertainty (real space) i0_real_error3.4390e+05
Rg (reciprocal space) rg_reciprocal22.12
I(0) (reciprocal space) i0_reciprocal21020000.0000
Solution quality estimate total_estimate0.8247
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.0
Skewness Skewness skewness0.467
Kurtosis Kurtosis kurtosis-0.124
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4839000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)