5gzg

Galectin-8 N-terminal domain carbohydrate recognition domain

Method: X-RAY DIFFRACTION Dmax: 58.0 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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–186 Fragment:carbohydrate recognition domain (UNP RESIDUES 1-186) beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 1 NA SODIUM ION × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.1M Tris pH 8.5, 0.01M NiCl2,20% (W/V) PEG2000 MME Resolution 2.00 Å R-free 0.258

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 4–189; UniProt 1–186

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 5gzg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5gzg
Deposition date deposition_date2016-09-28
Structure title titleGalectin-8 N-terminal domain carbohydrate recognition domain
Keywords keywordsGalectin-8 N-terminal domain carbohydrate recognition domain, 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_guinier16.01
Radius of gyration Rg (electron density) rg_electron14.44
Forward intensity I(0) i05395870.00
Molecular weight molecular_weight17147.0 kDa
Excluded volume excluded_volume21660 ų
Envelope volume envelope_volume24043 ų
Hydration-shell volume shell_volume13860 ų
Envelope diameter envelope_diameter50.0
Shell Rg shell_rg20.61
Envelope Rg envelope_rg14.76
Shape Rg shape_rg14.39
Total Rg total_rg15.79
Total atoms total_atoms1207
Residues n_residues149
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 dmax58.0
Rg (real space) rg_real15.87
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real5.3960e+06
I(0) uncertainty (real space) i0_real_error6.8730e+04
Rg (reciprocal space) rg_reciprocal15.88
I(0) (reciprocal space) i0_reciprocal5396000.0000
Solution quality estimate total_estimate0.8265
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.6
Skewness Skewness skewness0.016
Kurtosis Kurtosis kurtosis-0.455
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1126000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.584; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 1.000

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_idd5gzga_
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_id5gzgA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)