2yro

Solution structure of the C-terminal Gal-bind lectin protein from Human Galectin-8

Method: SOLUTION NMR Dmax: 55.4 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 175–316 Fragment:Gal-bind_lectin domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;296 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.28mM Gal-binding lectin U-15N, 13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O Resolution not provided

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 8–149; UniProt 175–316

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 2yro

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2yro
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2yro
Deposition date deposition_date2007-04-02
Structure title titleSolution structure of the C-terminal Gal-bind lectin protein from Human Galectin-8
Keywords keywords;Gal-bind lectin, galectin, sugar binding, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, SUGAR BINDING PROTEIN ;; SUGAR BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.04
Radius of gyration Rg (electron density) rg_electron15.29
Forward intensity I(0) i01605490000.00
Molecular weight molecular_weight340230.0 kDa
Excluded volume excluded_volume425800 ų
Envelope volume envelope_volume50669 ų
Hydration-shell volume shell_volume21653 ų
Envelope diameter envelope_diameter65.1
Shell Rg shell_rg26.15
Envelope Rg envelope_rg19.60
Shape Rg shape_rg15.26
Total Rg total_rg15.56
Total atoms total_atoms47740
Residues n_residues3100
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 dmax55.4
Rg (real space) rg_real15.94
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.6050e+09
I(0) uncertainty (real space) i0_real_error1.9130e+07
Rg (reciprocal space) rg_reciprocal15.95
I(0) (reciprocal space) i0_reciprocal1605000000.0000
Solution quality estimate total_estimate0.7715
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.209
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha732400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.676; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2yroa1
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_idd2yroa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2yroa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2yroA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)