5t7u

Crystal structure of galectin-8N in complex with Glycerol

Method: X-RAY DIFFRACTION Dmax: 46.4 Å Quality: REASONABLE

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 1–155 Fragment:N-terminal Domaine (UNP residues 1-155) Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 2 NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;10 mM sodium phosphate, 137 mM sodium chloride, 2.7 mM potassium chloride, 1.8 mM potassium phosphate Resolution 1.58 Å R-free 0.147

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 55 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 1–155; UniProt 1–155

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 5t7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5t7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5t7u
Deposition date deposition_date2016-09-05
Structure title titleCrystal structure of galectin-8N in complex with Glycerol
Keywords keywordscarbohydrate-binding protein, galectin-8 lectin, 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_guinier15.86
Radius of gyration Rg (electron density) rg_electron14.39
Forward intensity I(0) i05135570.00
Molecular weight molecular_weight16902.0 kDa
Excluded volume excluded_volume21425 ų
Envelope volume envelope_volume23703 ų
Hydration-shell volume shell_volume13705 ų
Envelope diameter envelope_diameter47.3
Shell Rg shell_rg20.55
Envelope Rg envelope_rg14.76
Shape Rg shape_rg14.36
Total Rg total_rg15.71
Total atoms total_atoms1191
Residues n_residues146
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 dmax46.4
Rg (real space) rg_real15.75
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real4.9680e+06
I(0) uncertainty (real space) i0_real_error4.2380e+04
Rg (reciprocal space) rg_reciprocal15.74
I(0) (reciprocal space) i0_reciprocal5136000.0000
Solution quality estimate total_estimate0.7062
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.058
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha12.1500
Highest regularization parameter α highest_alpha818600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 0.920; Sysdev: 0.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.611

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5t7ua_
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 (1 domains)

Domain ID domain_id5t7uA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)