8szk

The cryo-EM structure of PPP2R5A/HIV-1 Vif/CBFb/EloB/EloC complex

Method: ELECTRON MICROSCOPY Dmax: 118.3 Å Quality: GOOD

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

Elongin-B

Homo sapiens

UniProt Q15370

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–118 Not recorded Elongin-C × 1 (Q15369) Core-binding factor subunit beta × 1 (Q13951) Virion infectivity factor × 1 (P12504) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform × 1 (Q15172) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–118; UniProt 1–118

Elongin-C

Homo sapiens

UniProt Q15369

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) Core-binding factor subunit beta × 1 (Q13951) Virion infectivity factor × 1 (P12504) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform × 1 (Q15172) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–96; UniProt 17–112

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–187 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Virion infectivity factor × 1 (P12504) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform × 1 (Q15172) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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 Q13951-2
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 15–201; UniProt 1–187

Virion infectivity factor

Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 1–176 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Core-binding factor subunit beta × 1 (Q13951) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform × 1 (Q15172) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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 4
Chains and sequence ranges Author chain G; PDBConstruct 1–176; UniProt 1–176

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform

Homo sapiens

UniProt Q15172

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–486 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Core-binding factor subunit beta × 1 (Q13951) Virion infectivity factor × 1 (P12504) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2A5A_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–486; UniProt 1–486

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 8szk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8szk
Deposition date deposition_date2023-05-30
Structure title titleThe cryo-EM structure of PPP2R5A/HIV-1 Vif/CBFb/EloB/EloC complex
Keywords keywordsHIV Vif, Cul5 E3 ligase, PPP2R5A, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.30
Radius of gyration Rg (electron density) rg_electron34.67
Forward intensity I(0) i0163757000.00
Molecular weight molecular_weight104760.0 kDa
Excluded volume excluded_volume132150 ų
Envelope volume envelope_volume181920 ų
Hydration-shell volume shell_volume44438 ų
Envelope diameter envelope_diameter128.0
Shell Rg shell_rg40.63
Envelope Rg envelope_rg34.20
Shape Rg shape_rg34.64
Total Rg total_rg35.28
Total atoms total_atoms7392
Residues n_residues904
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 dmax118.3
Rg (real space) rg_real35.25
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real1.6380e+08
I(0) uncertainty (real space) i0_real_error2.6820e+06
Rg (reciprocal space) rg_reciprocal35.28
I(0) (reciprocal space) i0_reciprocal163800000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.1
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46400000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)