SAXSdb — 1c1f

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

PROTEIN (CONGERIN I)

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	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–135	Fragment：CARBOHYDRATE-RECOGNITION-DOMAIN Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 9；pH 9.0	Resolution 1.60 Å R-free 0.247

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 1C1F	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1C1L LACTOSE-LIGANDED CONGERIN I Deposited 1999-03-03	Different oligomeric state Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–135（135 aa） Fragment：CARBOHYDRATE-RECOGNITION-DOMAIN	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；pH 9.0	Resolution 1.50 Å R-free 0.265

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

View Construct and Data Evidence

UniProt name	LEG1_CONMY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–137； UniProt 1–135

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	1c1f
Deposition date deposition_date	1999-03-03
Structure title title	LIGAND-FREE CONGERIN I
Keywords keywords	GALECTIN, LECTIN, BETA-GALACTOSE-BINDING, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
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	15.47 Å
Radius of gyration Rg (electron density) rg_electron	14.08 Å
Forward intensity I(0) i0	4488270.00
Molecular weight molecular_weight	15226.0 kDa
Excluded volume excluded_volume	19074 Å³
Envelope volume envelope_volume	21233 Å³
Hydration-shell volume shell_volume	12770 Å³
Envelope diameter envelope_diameter	49.0 Å
Shell Rg shell_rg	19.96 Å
Envelope Rg envelope_rg	14.28 Å
Shape Rg shape_rg	14.06 Å
Total Rg total_rg	15.33 Å
Total atoms total_atoms	1078
Residues n_residues	135
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	53.4 Å
Rg (real space) rg_real	15.36 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	4.4880e+06
I(0) uncertainty (real space) i0_real_error	5.1390e+04
Rg (reciprocal space) rg_reciprocal	15.37 Å
I(0) (reciprocal space) i0_reciprocal	4488000.0000
Solution quality estimate total_estimate	0.7811
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	51.3 Å
Skewness Skewness skewness	0.059
Kurtosis Kurtosis kurtosis	-0.432
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	810200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1c1fa_
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 (1 domains)

Domain ID domain_id	1c1fA00
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	94.340 Å
Unit-cell length b length_b	36.920 Å
Unit-cell length c length_c	40.540 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	—
R_work r_work	0.2010
R_free r_free	0.2470

Description description	PROTEIN (CONGERIN I)
Molecular weight formula_weight	15356.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1163

LIGAND-FREE CONGERIN I

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

PROTEIN (CONGERIN I)

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	81

fit	/app/data/saxs_computation/c1/1c1f/1c1f.fit
pddf	/app/data/pr_computation/c1/1c1f/1c1f.pr.out
profile	/app/data/saxs_computation/c1/1c1f/1c1f.dat