SAXSdb — 5lxn

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

Transforming acidic coiled-coil-containing protein 3

Homo sapiens

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 758–838 Chain B； UniProt 758–838	Non-standard monomer：Yes (specific site not provided by mmCIF)	PGE TRIETHYLENE GLYCOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.08 Å R-free 0.285
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 758–838 Chain D； UniProt 758–838	Non-standard monomer：Yes (specific site not provided by mmCIF)	PGE TRIETHYLENE GLYCOL × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.08 Å R-free 0.285
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 758–838 Chain F； UniProt 758–838	Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.08 Å R-free 0.285
4	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 758–838 Chain H； UniProt 758–838	Non-standard monomer：Yes (specific site not provided by mmCIF)	PGE TRIETHYLENE GLYCOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.08 Å R-free 0.285

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 5LXN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5LXO Coiled-coil protein Deposited 2016-09-22	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 758–838（81 aa） Chain B 758–838（81 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1 PGE TRIETHYLENE GLYCOL × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.18 Å R-free 0.285
5LXO Coiled-coil protein Deposited 2016-09-22	Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 758–838（81 aa） Chain D 758–838（81 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.18 Å R-free 0.285
5LXO Coiled-coil protein Deposited 2016-09-22	Different ligand/ion Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 758–838（81 aa） Chain F 758–838（81 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.18 Å R-free 0.285
5LXO Coiled-coil protein Deposited 2016-09-22	Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 758–838（81 aa） Chain H 758–838（81 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289.15 K；35 % PEG 400, 0.05 M Sodium sulphate, 0.05 M Lithium sulphate, 0.05 M Tris pH 8.5	Resolution 2.18 Å R-free 0.285
5ODT Aurora-A in complex with TACC3 Deposited 2017-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 519–563（45 aa） Fragment：UNP residues 519-563	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；292 K；0.1 M Bis-Tris pH 5.5, 2 M Ammonium sulphate	Resolution 2.02 Å R-free 0.211
9YDY C-terminal coiled coil dimer of human TACC3 Deposited 2025-09-23	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 758–838（81 aa） Chain B 758–838（81 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；0.1 M imidazole, 50% (+/-)-2-Methyl-2,4-pentanediol (MPD)	Resolution 2.30 Å R-free 0.264

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TACC3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–81； UniProt 758–838 Author chain B； PDBConstruct 1–81； UniProt 758–838 Author chain C； PDBConstruct 1–81； UniProt 758–838 Author chain D； PDBConstruct 1–81； UniProt 758–838 Author chain E； PDBConstruct 1–81； UniProt 758–838 Author chain F； PDBConstruct 1–81； UniProt 758–838 Author chain G； PDBConstruct 1–81； UniProt 758–838 Author chain H； PDBConstruct 1–81； UniProt 758–838

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	5lxn
Deposition date deposition_date	2016-09-22
Structure title title	Coiled-coil protein
Keywords keywords	Coiled coil protein, tacc3, fusion protein, cc2, fgfr fusion, fgfr3, fgfr, cancer, structural protein; STRUCTURAL 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	47.64 Å
Radius of gyration Rg (electron density) rg_electron	49.67 Å
Forward intensity I(0) i0	98023400.00
Molecular weight molecular_weight	75567.0 kDa
Excluded volume excluded_volume	92927 Å³
Envelope volume envelope_volume	142120 Å³
Hydration-shell volume shell_volume	29833 Å³
Envelope diameter envelope_diameter	215.3 Å
Shell Rg shell_rg	40.13 Å
Envelope Rg envelope_rg	51.25 Å
Shape Rg shape_rg	49.88 Å
Total Rg total_rg	48.49 Å
Total atoms total_atoms	5217
Residues n_residues	623
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	128.5 Å
Rg (real space) rg_real	43.32 Å
Rg uncertainty (real space) rg_real_error	0.50 Å
I(0) (real space) i0_real	9.3110e+07
I(0) uncertainty (real space) i0_real_error	1.3840e+06
Rg (reciprocal space) rg_reciprocal	47.65 Å
I(0) (reciprocal space) i0_reciprocal	97810000.0000
Solution quality estimate total_estimate	0.6726
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	0.409
Kurtosis Kurtosis kurtosis	-0.620
Angular range angular_range	— – 0.1650 Å⁻¹
Current regularization parameter α current_alpha	0.6470
Highest regularization parameter α highest_alpha	2795000.0000
Real-space data points n_real_points	34
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.012; Oscil: 0.981; Stabil: 0.988; Sysdev: 0.000; Positv: 1.000; Valcen: 0.843; Smooth: 0.000

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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	Transforming acidic coiled-coil-containing protein 3
Molecular weight formula_weight	9448.4 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	5817

TQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	461

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8. Citations (1)

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Unit-cell length a length_a	57.389 Å
Unit-cell length b length_b	76.780 Å
Unit-cell length c length_c	86.832 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.17 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

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

Resolution resolution	2.080 Å
Low-resolution limit resolution_low	28.759 Å
R factor r_factor	0.2291
R_work r_work	0.2269
R_free r_free	0.2854

fit	/app/data/saxs_computation/lx/5lxn/5lxn.fit
pddf	/app/data/pr_computation/lx/5lxn/5lxn.pr.out
profile	/app/data/saxs_computation/lx/5lxn/5lxn.dat

Coiled-coil protein

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

Transforming acidic coiled-coil-containing protein 3

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