8b7l

X-ray structure of Auranofin-horse spleen ferritin

Method: X-RAY DIFFRACTION Dmax: 74.2 Å Quality: GOOD

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

Ferritin light chain

OrganismNot specified

UniProt P02791

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain AAA; UniProt 2–175 Not recorded CD CADMIUM ION × 27 SO4 SULFATE ION × 3 AU GOLD ION × 3 CL CHLORIDE ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;293 K;0.8 M ammonium sulphate 0.1 M TrisHCl pH 7.4 60 mM cadmium sulphate Resolution 1.24 Å R-free 0.180

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.

138 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FRIL_HORSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; 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 8b7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8b7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8b7l
Deposition date deposition_date2022-09-30
Structure title titleX-ray structure of Auranofin-horse spleen ferritin
Keywords keywordsferritin, gold, encapsulation, auranofin, anticancer, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.72
Radius of gyration Rg (electron density) rg_electron18.63
Forward intensity I(0) i09604830.00
Molecular weight molecular_weight20870.0 kDa
Excluded volume excluded_volume24951 ų
Envelope volume envelope_volume29835 ų
Hydration-shell volume shell_volume14509 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg23.55
Envelope Rg envelope_rg18.96
Shape Rg shape_rg18.51
Total Rg total_rg19.69
Total atoms total_atoms1396
Residues n_residues172
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 dmax74.2
Rg (real space) rg_real19.84
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real9.6050e+06
I(0) uncertainty (real space) i0_real_error1.1900e+05
Rg (reciprocal space) rg_reciprocal19.82
I(0) (reciprocal space) i0_reciprocal9605000.0000
Solution quality estimate total_estimate0.7921
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.488
Kurtosis Kurtosis kurtosis-0.191
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1242000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.563; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.607; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)