4v1w

3D structure of horse spleen apoferritin determined by electron cryomicroscopy

Method: ELECTRON MICROSCOPY Dmax: 135.7 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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 2–175 Chain B; UniProt 2–175 Chain C; UniProt 2–175 Chain D; UniProt 2–175 Chain E; UniProt 2–175 Chain F; UniProt 2–175 Chain G; UniProt 2–175 Chain H; UniProt 2–175 Chain I; UniProt 2–175 Chain J; UniProt 2–175 Chain K; UniProt 2–175 Chain L; UniProt 2–175 Chain M; UniProt 2–175 Chain N; UniProt 2–175 Chain O; UniProt 2–175 Chain P; UniProt 2–175 Chain Q; UniProt 2–175 Chain R; UniProt 2–175 Chain S; UniProt 2–175 Chain T; UniProt 2–175 Chain U; UniProt 2–175 Chain V; UniProt 2–175 Chain W; UniProt 2–175 Chain X; UniProt 2–175 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:PBS;pH 7.4;PBS cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 4.70 Å

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 A; PDBConstruct 1–174; UniProt 2–175 Author chain B; PDBConstruct 1–174; UniProt 2–175 Author chain C; PDBConstruct 1–174; UniProt 2–175 Author chain D; PDBConstruct 1–174; UniProt 2–175 Author chain E; PDBConstruct 1–174; UniProt 2–175 Author chain F; PDBConstruct 1–174; UniProt 2–175 Author chain G; PDBConstruct 1–174; UniProt 2–175 Author chain H; PDBConstruct 1–174; UniProt 2–175 Author chain I; PDBConstruct 1–174; UniProt 2–175 Author chain J; PDBConstruct 1–174; UniProt 2–175 Author chain K; PDBConstruct 1–174; UniProt 2–175 Author chain L; PDBConstruct 1–174; UniProt 2–175 Author chain M; PDBConstruct 1–174; UniProt 2–175 Author chain N; PDBConstruct 1–174; UniProt 2–175 Author chain O; PDBConstruct 1–174; UniProt 2–175 Author chain P; PDBConstruct 1–174; UniProt 2–175 Author chain Q; PDBConstruct 1–174; UniProt 2–175 Author chain R; PDBConstruct 1–174; UniProt 2–175 Author chain S; PDBConstruct 1–174; UniProt 2–175 Author chain T; PDBConstruct 1–174; UniProt 2–175 Author chain U; PDBConstruct 1–174; UniProt 2–175 Author chain V; PDBConstruct 1–174; UniProt 2–175 Author chain W; PDBConstruct 1–174; UniProt 2–175 Author chain X; 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 4v1w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v1w
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4v1w
Deposition date deposition_date2014-10-02
Structure title title3D structure of horse spleen apoferritin determined by electron cryomicroscopy
Keywords keywordsSTORAGE PROTEIN, IRON STORAGE, IRON TRANSPORT, FERRITINS, APOFERRITINS, HORSES, METALS, SPLEEN; STORAGE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.76
Radius of gyration Rg (electron density) rg_electron52.83
Forward intensity I(0) i03123390000.00
Molecular weight molecular_weight464520.0 kDa
Excluded volume excluded_volume579940 ų
Envelope volume envelope_volume957260 ų
Hydration-shell volume shell_volume147620 ų
Envelope diameter envelope_diameter136.5
Shell Rg shell_rg63.57
Envelope Rg envelope_rg47.61
Shape Rg shape_rg52.81
Total Rg total_rg53.22
Total atoms total_atoms32736
Residues n_residues4080
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 dmax135.7
Rg (real space) rg_real53.22
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.1230e+09
I(0) uncertainty (real space) i0_real_error4.3160e+07
Rg (reciprocal space) rg_reciprocal54.19
I(0) (reciprocal space) i0_reciprocal3128000000.0000
Solution quality estimate total_estimate0.8025
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary88.9
Skewness Skewness skewness-0.383
Kurtosis Kurtosis kurtosis-0.644
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77300000000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)