9x6r

Crystal structure of Frog M-ferritin E130A_K168E_H169D mutant

Method: X-RAY DIFFRACTION Dmax: 66.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ferritin, middle subunit

Aquarana catesbeiana

UniProt P07798

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 2–175 Mutation:E130A,K168E,H169D MG MAGNESIUM ION × 120 CL CHLORIDE ION × 240 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;277 K;2.0 M MgCl2 and 100 mM Bicine (pH 9.0) Resolution 1.48 Å R-free 0.173

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FRI2_AQUCT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–174; UniProt 2–175

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9x6r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x6r
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9x6r
Deposition date deposition_date2025-10-15
最后修订 last_revision2026-04-15
Structure title titleCrystal structure of Frog M-ferritin E130A_K168E_H169D mutant
Keywords keywordsMetal binding protein, Metal transport and storage protein, METAL TRANSPORT; METAL TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.20
Radius of gyration Rg (electron density) rg_electron18.32
Forward intensity I(0) i08488360.00
Molecular weight molecular_weight20398.0 kDa
Excluded volume excluded_volume25011 ų
Envelope volume envelope_volume29404 ų
Hydration-shell volume shell_volume14404 ų
Envelope diameter envelope_diameter68.5
Shell Rg shell_rg23.25
Envelope Rg envelope_rg18.82
Shape Rg shape_rg18.24
Total Rg total_rg19.32
Total atoms total_atoms1418
Residues n_residues171
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax66.5
Rg (real space) rg_real19.35
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real8.4880e+06
I(0) uncertainty (real space) i0_real_error1.0420e+05
Rg (reciprocal space) rg_reciprocal19.33
I(0) (reciprocal space) i0_reciprocal8488000.0000
Solution quality estimate total_estimate0.7549
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.540
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1872000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.670; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)