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28yp

SpyTag-FtnA from E.Coli

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

Bacterial non-heme ferritin

Escherichia coli

UniProt P0A998

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 24 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
1eum 28yp 28yq 28yr 4xgs

5 assemblies

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name FTNA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 28–191； UniProt 2–165 Author chain B； PDBConstruct 28–191； UniProt 2–165 Author chain C； PDBConstruct 28–191； UniProt 2–165 Author chain D； PDBConstruct 28–191； UniProt 2–165 Author chain E； PDBConstruct 28–191； UniProt 2–165 Author chain F； PDBConstruct 28–191； UniProt 2–165 Author chain G； PDBConstruct 28–191； UniProt 2–165 Author chain H； PDBConstruct 28–191； UniProt 2–165 Author chain I； PDBConstruct 28–191； UniProt 2–165 Author chain J； PDBConstruct 28–191； UniProt 2–165 Author chain K； PDBConstruct 28–191； UniProt 2–165 Author chain L； PDBConstruct 28–191； UniProt 2–165 Author chain M； PDBConstruct 28–191； UniProt 2–165 Author chain N； PDBConstruct 28–191； UniProt 2–165 Author chain O； PDBConstruct 28–191； UniProt 2–165 Author chain P； PDBConstruct 28–191； UniProt 2–165 Author chain Q； PDBConstruct 28–191； UniProt 2–165 Author chain R； PDBConstruct 28–191； UniProt 2–165 Author chain S； PDBConstruct 28–191； UniProt 2–165 Author chain T； PDBConstruct 28–191； UniProt 2–165 Author chain U； PDBConstruct 28–191； UniProt 2–165 Author chain V； PDBConstruct 28–191； UniProt 2–165 Author chain W； PDBConstruct 28–191； UniProt 2–165 Author chain X； PDBConstruct 28–191； UniProt 2–165

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_id28yp
Deposition date deposition_date2026-03-02
Structure title titleSpyTag-FtnA from E.Coli
Keywords keywordsFerritin A, METAL BINDING PROTEIN; METAL BINDING PROTEIN
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.

28yp__assembly_1__model_1

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

Download this curve (.dat)

28yp__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.

28yp__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）53.89 Å
Rg (electron density)53.16 Å
Total Rg53.55 Å
Atom count32016
Residues3864
Excluded volume567220 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 28yp__assembly_1__model_1 24-meric （24） 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)