6vtp

Crystal structure of G16C human Galectin-7 mutant

Method: X-RAY DIFFRACTION Dmax: 66.0 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 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–136 Chain B; UniProt 2–136 Mutation:G16C GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295.15 K;0.1 M Sodium chloride, 0.1M Tris pH 8, 20 % PEG 3350, 15 % Glycerol Resolution 2.30 Å R-free 0.261

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 6vtp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6vtp
Deposition date deposition_date2020-02-13
Structure title titleCrystal structure of G16C human Galectin-7 mutant
Keywords keywordsHuman Galectin-7, 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_guinier21.27
Radius of gyration Rg (electron density) rg_electron19.91
Forward intensity I(0) i016384000.00
Molecular weight molecular_weight29864.0 kDa
Excluded volume excluded_volume37096 ų
Envelope volume envelope_volume43803 ų
Hydration-shell volume shell_volume18920 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg25.64
Envelope Rg envelope_rg19.97
Shape Rg shape_rg19.90
Total Rg total_rg20.72
Total atoms total_atoms2111
Residues n_residues267
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 dmax66.0
Rg (real space) rg_real21.24
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.6380e+07
I(0) uncertainty (real space) i0_real_error2.0120e+05
Rg (reciprocal space) rg_reciprocal21.25
I(0) (reciprocal space) i0_reciprocal16380000.0000
Solution quality estimate total_estimate0.9060
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.539
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2772000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)