8vud

Crystal structure of APOBEC3F-CD1

Method: X-RAY DIFFRACTION Dmax: 75.9 Å Quality: EXCELLENT

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

DNA dC->dU-editing enzyme APOBEC-3F

Homo sapiens

UniProt Q8IUX4

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–190 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Bis-Tris, pH 5.5, 1.8 M ammonium sulfate Resolution 2.60 Å R-free 0.239
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–190 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Bis-Tris, pH 5.5, 1.8 M ammonium sulfate Resolution 2.60 Å R-free 0.239

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.

9 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ABC3F_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–197; UniProt 1–190 Author chain B; PDBConstruct 8–197; UniProt 1–190

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 8vud

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vud
Deposition date deposition_date2024-01-29
Structure title titleCrystal structure of APOBEC3F-CD1
Keywords keywordsAPOBEC3F, HIV, Cytidine Deaminases, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.11
Radius of gyration Rg (electron density) rg_electron22.87
Forward intensity I(0) i034388300.00
Molecular weight molecular_weight44476.0 kDa
Excluded volume excluded_volume55186 ų
Envelope volume envelope_volume70143 ų
Hydration-shell volume shell_volume25406 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg29.92
Envelope Rg envelope_rg22.49
Shape Rg shape_rg22.81
Total Rg total_rg23.87
Total atoms total_atoms3122
Residues n_residues370
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 dmax75.9
Rg (real space) rg_real23.97
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.4390e+07
I(0) uncertainty (real space) i0_real_error4.1390e+05
Rg (reciprocal space) rg_reciprocal24.01
I(0) (reciprocal space) i0_reciprocal34390000.0000
Solution quality estimate total_estimate0.9039
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.8
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7354000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)