8pp3

Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and crystal contact tuned negatively supercharged ferritin variant Ftn(neg)-m1 (Mg formate condition)

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

Ferritin heavy chain

Homo sapiens

UniProt P02794

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 24 FE (III) ION × 24 GLYCEROL × 16 water × 24 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 24 FE (III) ION × 24 MAGNESIUM ION × 8 water × 24 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FRIH_HUMAN
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–183; UniProt 1–183 Author chain B; PDBConstruct 1–183; UniProt 1–183 Author chain C; PDBConstruct 1–183; UniProt 1–183 Author chain D; PDBConstruct 1–183; UniProt 1–183 Author chain E; PDBConstruct 1–183; UniProt 1–183 Author chain F; PDBConstruct 1–183; UniProt 1–183 Author chain G; PDBConstruct 1–183; UniProt 1–183 Author chain H; PDBConstruct 1–183; UniProt 1–183 Author chain I; PDBConstruct 1–183; UniProt 1–183 Author chain J; PDBConstruct 1–183; UniProt 1–183 Author chain K; PDBConstruct 1–183; UniProt 1–183 Author chain L; PDBConstruct 1–183; UniProt 1–183

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_id8pp3
Deposition date deposition_date2023-07-06
Structure title titleBinary crystal structure of positively supercharged ferritin variant Ftn(pos) and crystal contact tuned negatively supercharged ferritin variant Ftn(neg)-m1 (Mg formate condition)
Keywords keywords;protein design, protein engineering, protein interfaces, superlattice, nanocage, ferritin, protein container, charged nanocage, OXIDOREDUCTASE ;; OXIDOREDUCTASE
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.

8pp3__assembly_1__model_1

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

Download this curve (.dat)

8pp3__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.

8pp3__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)53.93 Å
Rg (electron density)53.07 Å
Total Rg53.48 Å
Atom count68912
Residues4128
Excluded volume610990 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8pp3__assembly_1__model_1 24-meric (24) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 8pp3__assembly_2__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 (6)

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7. Citations (1)