9e93

Structural Insights into HIV-1 Vif-Mediated Ubiquitination and Degradation of APOBEC3H

Method: ELECTRON MICROSCOPY Dmax: 101.5 Å Quality: GOOD

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

single-stranded DNA cytosine deaminase

Pan troglodytes

UniProt B7T0U6

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 × 6 RNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–183 Chain E; UniProt 1–183 Not recorded ;RNA (5'-R(P*UP*GP*CP*CP*GP*GP*GP*UP*A)-3') ; × 2 ;RNA (5'-R(*AP*UP*AP*CP*CP*CP*GP*GP*CP*A)-3') ; × 2 Core-binding factor subunit beta × 2 (Q13951) Virion infectivity factor × 2 (P12504) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B7T0U6_PANTR
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 3–185; UniProt 1–183 Author chain E; PDBConstruct 3–185; UniProt 1–183

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 × 6 RNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain o; UniProt 1–170 Chain s; UniProt 1–170 Not recorded ;RNA (5'-R(P*UP*GP*CP*CP*GP*GP*GP*UP*A)-3') ; × 2 ;RNA (5'-R(*AP*UP*AP*CP*CP*CP*GP*GP*CP*A)-3') ; × 2 single-stranded DNA cytosine deaminase × 2 (B7T0U6) Virion infectivity factor × 2 (P12504) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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 4
Chains and sequence ranges Author chain o; PDBConstruct 1–170; UniProt 1–170 Author chain s; PDBConstruct 1–170; UniProt 1–170

Virion infectivity factor

Human immunodeficiency virus 1

UniProt P12504

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 × 6 RNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain p; UniProt 1–176 Chain t; UniProt 1–176 Not recorded ;RNA (5'-R(P*UP*GP*CP*CP*GP*GP*GP*UP*A)-3') ; × 2 ;RNA (5'-R(*AP*UP*AP*CP*CP*CP*GP*GP*CP*A)-3') ; × 2 single-stranded DNA cytosine deaminase × 2 (B7T0U6) Core-binding factor subunit beta × 2 (Q13951) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VIF_HV1N5
Isoform
PDB entities 5
Chains and sequence ranges Author chain p; PDBConstruct 1–176; UniProt 1–176 Author chain t; PDBConstruct 1–176; UniProt 1–176

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 9e93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e93
Deposition date deposition_date2024-11-07
Structure title titleStructural Insights into HIV-1 Vif-Mediated Ubiquitination and Degradation of APOBEC3H
Keywords keywordsAPOBEC3H HIV-1 Vif, VIRAL PROTEIN, 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_guinier33.54
Radius of gyration Rg (electron density) rg_electron32.43
Forward intensity I(0) i0285286000.00
Molecular weight molecular_weight125520.0 kDa
Excluded volume excluded_volume152890 ų
Envelope volume envelope_volume208380 ų
Hydration-shell volume shell_volume51679 ų
Envelope diameter envelope_diameter104.8
Shell Rg shell_rg40.81
Envelope Rg envelope_rg32.28
Shape Rg shape_rg32.40
Total Rg total_rg33.14
Total atoms total_atoms8773
Residues n_residues1003
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 dmax101.5
Rg (real space) rg_real33.32
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.8530e+08
I(0) uncertainty (real space) i0_real_error4.3830e+06
Rg (reciprocal space) rg_reciprocal33.46
I(0) (reciprocal space) i0_reciprocal285300000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.4
Skewness Skewness skewness0.027
Kurtosis Kurtosis kurtosis-0.533
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38740000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)