2v2o

Mutant R59M recombinant horse spleen apoferritin cocrystallized with haemin in basic conditions

Method: X-RAY DIFFRACTION Dmax: 69.6 Å Quality: REASONABLE

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

FERRITIN LIGHT CHAIN

EQUUS CABALLUS

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 1–174 Mutation:YES CD CADMIUM ION × 216 GOL GLYCEROL × 24 SO4 SULFATE ION × 24 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;RESERVOIR: CADMIUM SULFATE 0.145M, AMMONIUM SULFATE 0.55M, SODIUM AZIDE 0.003M. DROP: 1UL PROTEIN AND 1UL RESERVOIR, pH 8.2 Resolution 1.87 Å R-free 0.236

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 1–174

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 2v2o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2v2o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2v2o
Deposition date deposition_date2007-06-06
Structure title titleMutant R59M recombinant horse spleen apoferritin cocrystallized with haemin in basic conditions
Keywords keywordsMETAL TRANSPORT, IRON, IRON STORAGE, METAL-BINDING; METAL TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.76
Radius of gyration Rg (electron density) rg_electron18.60
Forward intensity I(0) i09179340.00
Molecular weight molecular_weight20600.0 kDa
Excluded volume excluded_volume24762 ų
Envelope volume envelope_volume29351 ų
Hydration-shell volume shell_volume14339 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg23.42
Envelope Rg envelope_rg18.92
Shape Rg shape_rg18.45
Total Rg total_rg19.70
Total atoms total_atoms1386
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 dmax69.6
Rg (real space) rg_real19.87
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real9.1790e+06
I(0) uncertainty (real space) i0_real_error1.3990e+05
Rg (reciprocal space) rg_reciprocal19.86
I(0) (reciprocal space) i0_reciprocal9179000.0000
Solution quality estimate total_estimate0.6017
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.6
Skewness Skewness skewness0.477
Kurtosis Kurtosis kurtosis-0.242
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1153000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.674; Stabil: 0.997; Sysdev: 0.338; Positv: 1.000; Valcen: 0.793; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2v2oa_
Class classa — All alpha proteins
Fold Fold folda.25 — Ferritin-like
Superfamily Superfamily superfamilya.25.1 — Ferritin-like
Family Family familya.25.1.1 — Ferritin

CATH v4.4 (1 domains)

Domain ID domain_id2v2oA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1260 — Ferritin
Homologous superfamily homologous superfamily10 — Ferritin, core subunit, four-helix bundle

8. Citations (1)

9. Files and Curves (10)