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9v5h

cryo-EM structure of hexameric ArnA

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

Bifunctional polymyxin resistance protein ArnA

Escherichia coli

UniProt P77398

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 12 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1u9j 1yrw 1z73 1z74 1z75 1z7b 2bln 2bln

8 assemblies

Homodimer
1u9j 2bll

2 assemblies

Homotetramer

None

Other homooligomers
1u9j 1z73 1z75 1z7e 21ak 4wkg 9v5h 9wi0

8 assemblies

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name ARNA_ECOLI
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A； PDBConstruct 1–300； UniProt 1–300 Author chain B； PDBConstruct 1–300； UniProt 1–300 Author chain C； PDBConstruct 1–300； UniProt 1–300 Author chain D； PDBConstruct 1–300； UniProt 1–300 Author chain E； PDBConstruct 1–300； UniProt 1–300 Author chain F； PDBConstruct 1–300； UniProt 1–300 Author chain G； PDBConstruct 2–342； UniProt 317–657 Author chain H； PDBConstruct 2–342； UniProt 317–657 Author chain I； PDBConstruct 2–342； UniProt 317–657 Author chain J； PDBConstruct 2–342； UniProt 317–657 Author chain K； PDBConstruct 2–342； UniProt 317–657 Author chain L； PDBConstruct 2–342； UniProt 317–657

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_id9v5h
Deposition date deposition_date2025-05-26
Structure title titlecryo-EM structure of hexameric ArnA
Keywords keywords;Lipid A modification Polymyxin resistance Bifunctional enzyme UDP-glucuronic acid dehydrogenase UDP-4-amino-4-deoxy-L-arabinose, transferase Lipopolysaccharide biosynthesis Antibiotic resistance Aminotransferase Dehydrogenase LPS modification pathway L-Ara4N biosynthesis, TRANSFERASE ;; TRANSFERASE
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.

9v5h__assembly_1__model_1

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

Download this curve (.dat)

9v5h__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.

9v5h__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）52.24 Å
Rg (electron density)51.61 Å
Total Rg52.00 Å
Atom count29508
Residues3726
Excluded volume525480 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9v5h__assembly_1__model_1 dodecameric （12） 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 (2)

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7. Citations (2)