6vtq

Crystal structure of G16C human Galectin-7 mutant in complex with lactose

Method: X-RAY DIFFRACTION Dmax: 66.8 Å Quality: EXCELLENT

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

Galectin-7

Homo sapiens

UniProt P47929

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–136 Chain B; UniProt 2–136 Mutation:G16C Non-standard monomer:Yes (specific site not provided by mmCIF) beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295.15 K;0.1 M Tris pH 8, 0.1 M Sodium Chloride, 25 % PEG3350, 7.5 mM alpha-lactose Resolution 1.95 Å R-free 0.244

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.

34 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LEG7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain B; PDBConstruct 1–135; UniProt 2–136

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 6vtq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vtq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6vtq
Deposition date deposition_date2020-02-13
Structure title titleCrystal structure of G16C human Galectin-7 mutant in complex with lactose
Keywords keywordsHuman Galectin-7, lactose, G16C mutant, disulfide bond, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.54
Radius of gyration Rg (electron density) rg_electron20.15
Forward intensity I(0) i016933900.00
Molecular weight molecular_weight30284.0 kDa
Excluded volume excluded_volume37600 ų
Envelope volume envelope_volume44890 ų
Hydration-shell volume shell_volume19193 ų
Envelope diameter envelope_diameter67.6
Shell Rg shell_rg25.98
Envelope Rg envelope_rg20.28
Shape Rg shape_rg20.12
Total Rg total_rg21.03
Total atoms total_atoms4233
Residues n_residues262
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 dmax66.8
Rg (real space) rg_real21.53
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.6930e+07
I(0) uncertainty (real space) i0_real_error1.8500e+05
Rg (reciprocal space) rg_reciprocal21.53
I(0) (reciprocal space) i0_reciprocal16930000.0000
Solution quality estimate total_estimate0.9058
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.509
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2861000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)