6nil

cryoEM structure of the truncated HIV-1 Vif/CBFbeta/A3F complex

Method: ELECTRON MICROSCOPY Dmax: 124.9 Å Quality: GOOD

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 Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 185–373 Chain D; UniProt 185–373 Chain G; UniProt 185–373 Chain J; UniProt 185–373 Fragment:C-terminal domain Mutation:Y196D, H247G, C248R, F302K, W310K, Y314A, Q315A, K355D, K358D, F363D Core-binding factor subunit beta × 4 (Q13951) Virion infectivity factor × 4 (P12504,A0A346ARH7) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

9 other PDB entries and 19 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 19–207; UniProt 185–373 Author chain D; PDBConstruct 19–207; UniProt 185–373 Author chain G; PDBConstruct 19–207; UniProt 185–373 Author chain J; PDBConstruct 19–207; UniProt 185–373

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 Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–151 Chain E; UniProt 1–151 Chain H; UniProt 1–151 Chain K; UniProt 1–151 Not recorded DNA dC->dU-editing enzyme APOBEC-3F × 4 (Q8IUX4) Virion infectivity factor × 4 (P12504,A0A346ARH7) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–151; UniProt 1–151 Author chain E; PDBConstruct 1–151; UniProt 1–151 Author chain H; PDBConstruct 1–151; UniProt 1–151 Author chain K; PDBConstruct 1–151; UniProt 1–151

Virion infectivity factor

Human immunodeficiency virus 1

UniProt A0A346ARH7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 158–176 Chain F; UniProt 158–176 Chain I; UniProt 158–176 Chain L; UniProt 158–176 Not recorded DNA dC->dU-editing enzyme APOBEC-3F × 4 (Q8IUX4) Core-binding factor subunit beta × 4 (Q13951) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 A0A346ARH7_9HIV1
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 120–138; UniProt 158–176 Author chain F; PDBConstruct 120–138; UniProt 158–176 Author chain I; PDBConstruct 120–138; UniProt 158–176 Author chain L; PDBConstruct 120–138; UniProt 158–176

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 Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–113 Chain F; UniProt 1–113 Chain I; UniProt 1–113 Chain L; UniProt 1–113 Not recorded DNA dC->dU-editing enzyme APOBEC-3F × 4 (Q8IUX4) Core-binding factor subunit beta × 4 (Q13951) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–113; UniProt 1–113 Author chain F; PDBConstruct 1–113; UniProt 1–113 Author chain I; PDBConstruct 1–113; UniProt 1–113 Author chain L; PDBConstruct 1–113; UniProt 1–113

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 6nil

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6nil
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6nil
Deposition date deposition_date2018-12-29
Structure title titlecryoEM structure of the truncated HIV-1 Vif/CBFbeta/A3F complex
Keywords keywordsHuman antiviral restriction factor, HIV viral protein, ANTIVIRAL PROTEIN; ANTIVIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.35
Radius of gyration Rg (electron density) rg_electron39.37
Forward intensity I(0) i0717429000.00
Molecular weight molecular_weight215610.0 kDa
Excluded volume excluded_volume267990 ų
Envelope volume envelope_volume382110 ų
Hydration-shell volume shell_volume77946 ų
Envelope diameter envelope_diameter126.7
Shell Rg shell_rg47.68
Envelope Rg envelope_rg38.16
Shape Rg shape_rg39.35
Total Rg total_rg39.91
Total atoms total_atoms15220
Residues n_residues1800
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 dmax124.9
Rg (real space) rg_real40.12
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real7.1740e+08
I(0) uncertainty (real space) i0_real_error1.0430e+07
Rg (reciprocal space) rg_reciprocal40.35
I(0) (reciprocal space) i0_reciprocal717600000.0000
Solution quality estimate total_estimate0.8932
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.4
Skewness Skewness skewness0.068
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha223300000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6nilB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology250 — Polyomavirus Enhancer Binding Protein 2; Chain: A;
Homologous superfamily homologous superfamily10 — Core binding factor, beta subunit
Domain ID domain_id6nilE00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology250 — Polyomavirus Enhancer Binding Protein 2; Chain: A;
Homologous superfamily homologous superfamily10 — Core binding factor, beta subunit
Domain ID domain_id6nilH00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology250 — Polyomavirus Enhancer Binding Protein 2; Chain: A;
Homologous superfamily homologous superfamily10 — Core binding factor, beta subunit
Domain ID domain_id6nilK00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology250 — Polyomavirus Enhancer Binding Protein 2; Chain: A;
Homologous superfamily homologous superfamily10 — Core binding factor, beta subunit

8. Citations (1)

9. Files and Curves (10)