3f33

Apoferritin: complex with propofol

Method: X-RAY DIFFRACTION Dmax: 72.7 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 Not recorded CD CADMIUM ION × 144 PFL 2,6-BIS(1-METHYLETHYL)PHENOL × 24 SO4 SULFATE ION × 24 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;Cadmium sulfate, ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.70 Å R-free 0.220

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

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 3f33

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3f33
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3f33
Deposition date deposition_date2008-10-30
Structure title titleApoferritin: complex with propofol
Keywords keywords4-helix bundle, anesthetic, propofol, Acetylation, Iron, Iron storage, Metal-binding, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.51
Radius of gyration Rg (electron density) rg_electron18.34
Forward intensity I(0) i08323780.00
Molecular weight molecular_weight20160.0 kDa
Excluded volume excluded_volume24626 ų
Envelope volume envelope_volume29018 ų
Hydration-shell volume shell_volume14334 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg23.31
Envelope Rg envelope_rg18.69
Shape Rg shape_rg18.22
Total Rg total_rg19.44
Total atoms total_atoms1378
Residues n_residues168
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 dmax72.7
Rg (real space) rg_real19.63
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real8.3240e+06
I(0) uncertainty (real space) i0_real_error1.1170e+05
Rg (reciprocal space) rg_reciprocal19.61
I(0) (reciprocal space) i0_reciprocal8324000.0000
Solution quality estimate total_estimate0.7982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1258000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.574; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.655; Smooth: 0.996

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_idd3f33a_
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_id3f33A00
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)