9qg1

Natively purified Rubrerythrin 16-mer from the anaerobic extremophile P. furiosus

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

Rubrerythrin

OrganismNot specified

UniProt Q9UWP7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 16 FE (III) ION × 48 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q9UWP7_9EURY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–171; UniProt 1–171 Author chain B; PDBConstruct 1–171; UniProt 1–171 Author chain C; PDBConstruct 1–171; UniProt 1–171 Author chain D; PDBConstruct 1–171; UniProt 1–171 Author chain E; PDBConstruct 1–171; UniProt 1–171 Author chain F; PDBConstruct 1–171; UniProt 1–171 Author chain G; PDBConstruct 1–171; UniProt 1–171 Author chain H; PDBConstruct 1–171; UniProt 1–171 Author chain I; PDBConstruct 1–171; UniProt 1–171 Author chain J; PDBConstruct 1–171; UniProt 1–171 Author chain K; PDBConstruct 1–171; UniProt 1–171 Author chain L; PDBConstruct 1–171; UniProt 1–171 Author chain M; PDBConstruct 1–171; UniProt 1–171 Author chain N; PDBConstruct 1–171; UniProt 1–171 Author chain O; PDBConstruct 1–171; UniProt 1–171 Author chain P; PDBConstruct 1–171; UniProt 1–171

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_id9qg1
Deposition date deposition_date2025-03-13
Last revision last_revision2025-07-16
Structure title titleNatively purified Rubrerythrin 16-mer from the anaerobic extremophile P. furiosus
Keywords keywordsMetalloprotein, oxidotic stress response, ferritin-like, rubredoxin domain., OXIDOREDUCTASE; OXIDOREDUCTASE
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.

9qg1__assembly_1__model_1

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

Download this curve (.dat)

9qg1__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.

9qg1__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)62.21 Å
Rg (electron density)62.13 Å
Total Rg62.17 Å
Atom count21968
Residues2736
Excluded volume395750 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9qg1__assembly_1__model_1 16-meric (16) 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 (1)