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9sie

Structure of the bacterial archaellum from L. aerophila

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Flagellin

OrganismNot specified

UniProt A0A540VDN8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 17 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer

None

Other homooligomers
9i5h 9r50 9sie 9sii

4 assemblies

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name A0A540VDN8_9CHLR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain C； PDBConstruct 1–183； UniProt 29–211 Author chain D； PDBConstruct 1–183； UniProt 29–211 Author chain E； PDBConstruct 1–183； UniProt 29–211 Author chain F； PDBConstruct 1–183； UniProt 29–211 Author chain G； PDBConstruct 1–183； UniProt 29–211 Author chain H； PDBConstruct 1–183； UniProt 29–211 Author chain I； PDBConstruct 1–183； UniProt 29–211 Author chain J； PDBConstruct 1–183； UniProt 29–211 Author chain K； PDBConstruct 1–183； UniProt 29–211 Author chain L； PDBConstruct 1–183； UniProt 29–211 Author chain M； PDBConstruct 1–183； UniProt 29–211 Author chain N； PDBConstruct 1–183； UniProt 29–211 Author chain O； PDBConstruct 1–183； UniProt 29–211 Author chain P； PDBConstruct 1–183； UniProt 29–211 Author chain Q； PDBConstruct 1–183； UniProt 29–211 Author chain R； PDBConstruct 1–183； UniProt 29–211 Author chain S； PDBConstruct 1–183； UniProt 29–211

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_id9sie
Deposition date deposition_date2025-08-28
Structure title titleStructure of the bacterial archaellum from L. aerophila
Keywords keywordsHelical, cell surface structure, motility, archaellum, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY
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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.

9sie__assembly_1__model_1

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

Download this curve (.dat)

9sie__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9sie__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）48.59 Å
Rg (electron density)48.92 Å
Total Rg49.23 Å
Atom count23324
Residues3111
Excluded volume416290 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9sie__assembly_1__model_1 17-meric （17） 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 (1)

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7. Citations (1)