SAXSdb — 1a78

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

GALECTIN-1

OrganismNot specified

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 Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–134 Chain B； UniProt 1–134	Not recorded	beta-D-galactopyranose-(1-1)-1-thio-beta-D-galactopyranose × 2 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.6；DROPS OF EQUAL AMOUNT OF 10-12 MG/ML PROTEIN AND RESERVOIR SOLUTION WERE EQUILIBRATED AGAINST 1 ML OF (NH4)2SO4 AT 56% SATURATION IN 100MM TRIS-ACETATE BUFFER, PH 6.6 AND 1% MPD AND 1% DTT	Resolution 2.00 Å R-free 0.256

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.

Other PDB	Difference from Current Entry 1A78	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GAN COMPLEX OF TOAD OVARY GALECTIN WITH N-ACETYLGALACTOSE Deposited 1996-11-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–134（134 aa） Chain B 1–134（134 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.6；DROPS OF EQUAL AMOUNT OF 10-12 MG/ML PROTEIN AND RESERVOIR SOLUTION WERE EQUILIBRATED AGAINST 1 ML OF (NH4)2SO4 AT 56% SATURATION IN 100MM TRIS-ACETATE BUFFER, PH 6.6 AND 1% MPD AND 1% DTT	Resolution 2.23 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LEG1_BUFAR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–134； UniProt 1–134 Author chain B； PDBConstruct 1–134； UniProt 1–134

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1a78
Deposition date deposition_date	1998-03-20
Structure title title	COMPLEX OF TOAD OVARY GALECTIN WITH THIO-DIGALACTOSE
Keywords keywords	S-LECTIN, CARBOHYDRATE BINDING, COMPLEX (LECTIN-SACCHARIDE), LECTIN; LECTIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	21.19 Å
Radius of gyration Rg (electron density) rg_electron	20.10 Å
Forward intensity I(0) i0	15663000.00
Molecular weight molecular_weight	30286.0 kDa
Excluded volume excluded_volume	38007 Å³
Envelope volume envelope_volume	43576 Å³
Hydration-shell volume shell_volume	18699 Å³
Envelope diameter envelope_diameter	66.2 Å
Shell Rg shell_rg	25.46 Å
Envelope Rg envelope_rg	20.07 Å
Shape Rg shape_rg	20.11 Å
Total Rg total_rg	20.82 Å
Total atoms total_atoms	2128
Residues n_residues	268
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	66.2 Å
Rg (real space) rg_real	21.17 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	1.5660e+07
I(0) uncertainty (real space) i0_real_error	2.0620e+05
Rg (reciprocal space) rg_reciprocal	21.18 Å
I(0) (reciprocal space) i0_reciprocal	15660000.0000
Solution quality estimate total_estimate	0.9040
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.4 Å
Skewness Skewness skewness	0.301
Kurtosis Kurtosis kurtosis	-0.517
Angular range angular_range	— – 0.3750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3010000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.989

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GALECTIN-1
Molecular weight formula_weight	14725.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2174

ASAGVAVTNLNLKPGHCVEIKGSIPPDCKGFAVNLGEDASNFLLHFNARFDLHGDVNKIVCNSKEADAWGSEQREEVFPFQQGAEVMVCFEYQTQKIIIKFSSGDQFSFPVRKVLPSIPFLSLEGLAFKSITTE

Entity 2 Entity 2 branched

Description description	beta-D-galactopyranose-(1-1)-1-thio-beta-D-galactopyranose
Molecular weight formula_weight	358.4 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2,3-DIHYDROXY-1,4-DITHIOBUTANE
Molecular weight formula_weight	154.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	46

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1a78a_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.3 — Galectin (animal S-lectin)

Domain ID domain_id	d1a78b_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.3 — Galectin (animal S-lectin)

CATH v4.4 (2 domains)

Domain ID domain_id	1a78A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	1a78B00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

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8. Citations (1)

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Unit-cell length a length_a	51.800 Å
Unit-cell length b length_b	51.000 Å
Unit-cell length c length_c	56.300 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.20 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.1940
R_work r_work	0.1940
R_free r_free	0.2560

fit	/app/data/saxs_computation/a7/1a78/1a78.fit
pddf	/app/data/pr_computation/a7/1a78/1a78.pr.out
profile	/app/data/saxs_computation/a7/1a78/1a78.dat

COMPLEX OF TOAD OVARY GALECTIN WITH THIO-DIGALACTOSE

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

GALECTIN-1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction