3vkn

Galectin-8 N-terminal domain in free form

Method: X-RAY DIFFRACTION Dmax: 76.0 Å Quality: GOOD

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

Galectin-8

Homo sapiens

UniProt O00214

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–153 Fragment:N-TERMINAL CARBOHYDRATE RECOGNITION DOMAIN CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.5;293 K;30%(v/v) PEG 400, 0.1M CHES, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.98 Å R-free 0.251
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–153 Fragment:N-TERMINAL CARBOHYDRATE RECOGNITION DOMAIN No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.5;293 K;30%(v/v) PEG 400, 0.1M CHES, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.98 Å R-free 0.251

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.

36 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LEG8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 1–153 Author chain B; PDBConstruct 1–153; UniProt 1–153

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 3vkn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3vkn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3vkn
Deposition date deposition_date2011-11-18
Structure title titleGalectin-8 N-terminal domain in free form
Keywords keywordsbete-sandwich, carbohydrate binding, oligosaccharide, 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_guinier23.37
Radius of gyration Rg (electron density) rg_electron22.33
Forward intensity I(0) i018259900.00
Molecular weight molecular_weight33352.0 kDa
Excluded volume excluded_volume42202 ų
Envelope volume envelope_volume50513 ų
Hydration-shell volume shell_volume19491 ų
Envelope diameter envelope_diameter76.6
Shell Rg shell_rg28.31
Envelope Rg envelope_rg22.41
Shape Rg shape_rg22.28
Total Rg total_rg23.32
Total atoms total_atoms2355
Residues n_residues294
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 dmax76.0
Rg (real space) rg_real23.42
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.8260e+07
I(0) uncertainty (real space) i0_real_error2.7750e+05
Rg (reciprocal space) rg_reciprocal23.41
I(0) (reciprocal space) i0_reciprocal18260000.0000
Solution quality estimate total_estimate0.8890
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.343
Kurtosis Kurtosis kurtosis-0.555
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3438000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3vkna_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.0 — automated matches
Domain ID domain_idd3vknb_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3vknA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id3vknB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)