8e40

Full-length APOBEC3G in complex with HIV-1 Vif, CBF-beta, and fork RNA

Method: ELECTRON MICROSCOPY Dmax: 118.8 Å Quality: GOOD

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

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

Macaca mulatta

UniProt Q7YR23

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–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 1–370 Not recorded Virion infectivity factor × 1 (B2CPZ0) Core-binding factor subunit beta × 1 (Q13951) RNA × 1 RNA × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ABC3G_MACMU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–380; UniProt 1–370

Virion infectivity factor

Human immunodeficiency virus 1

UniProt B2CPZ0

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–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain B; UniProt 1–176 Fragment:UNP residues 1-176 DNA dC->dU-editing enzyme APOBEC-3G × 1 (Q7YR23) Core-binding factor subunit beta × 1 (Q13951) RNA × 1 RNA × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name B2CPZ0_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–178; UniProt 1–176

Core-binding factor subunit beta

Homo sapiens

UniProt Q13951

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–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain C; UniProt 1–157 Fragment:UNP residues 1-157 DNA dC->dU-editing enzyme APOBEC-3G × 1 (Q7YR23) Virion infectivity factor × 1 (B2CPZ0) RNA × 1 RNA × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

19 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PEBB_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–157; UniProt 1–157

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 8e40

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e40
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e40
Deposition date deposition_date2022-08-17
Structure title titleFull-length APOBEC3G in complex with HIV-1 Vif, CBF-beta, and fork RNA
Keywords keywordsViral protein - human protein complex, ribonucleoprotein complex, VIRAL PROTEIN-RNA complex; VIRAL PROTEIN/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.17
Radius of gyration Rg (electron density) rg_electron32.40
Forward intensity I(0) i0163706000.00
Molecular weight molecular_weight90263.0 kDa
Excluded volume excluded_volume107800 ų
Envelope volume envelope_volume145900 ų
Hydration-shell volume shell_volume39084 ų
Envelope diameter envelope_diameter125.2
Shell Rg shell_rg37.58
Envelope Rg envelope_rg32.67
Shape Rg shape_rg32.30
Total Rg total_rg33.07
Total atoms total_atoms6297
Residues n_residues683
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 dmax118.8
Rg (real space) rg_real34.25
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real1.6370e+08
I(0) uncertainty (real space) i0_real_error2.7770e+06
Rg (reciprocal space) rg_reciprocal34.20
I(0) (reciprocal space) i0_reciprocal163700000.0000
Solution quality estimate total_estimate0.8767
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.3
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.229
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17780000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.941

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8e40A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2

8. Citations (1)

9. Files and Curves (10)