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5lxn

Coiled-coil protein

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Transforming acidic coiled-coil-containing protein 3

Homo sapiens

UniProt Q9Y6A5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 TRIETHYLENE GLYCOL × 3 water × 2 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 2 TRIETHYLENE GLYCOL × 1 SULFATE ION × 2 water × 2 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 2 water × 2 Consistent with protein count
4 Protein homooligomer Homooligomer Protein 2 TRIETHYLENE GLYCOL × 3 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer
5lxn 5lxn 5lxn 5lxn 5lxo 5lxo 5lxo 5lxo 9ydy

9 assemblies

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
5odt

1 assemblies

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_id5lxn
Deposition date deposition_date2016-09-22
Structure title titleCoiled-coil protein
Keywords keywordsCoiled coil protein, tacc3, fusion protein, cc2, fgfr fusion, fgfr3, fgfr, cancer, structural protein; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5lxn__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5lxn__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5lxn__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）33.26 Å
Rg (electron density)35.12 Å
Total Rg34.65 Å
Atom count1325
Residues157
Excluded volume23661 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5lxn__assembly_1__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 5lxn__assembly_2__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 5lxn__assembly_3__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 5lxn__assembly_4__model_1 dimeric （2） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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7. Citations (1)