6xqi

Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A

Method: X-RAY DIFFRACTION Dmax: 84.9 Å Quality: GOOD

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

Protein Vpr

Human immunodeficiency virus type 1 group M subtype B (isolate NY5)

UniProt P12520

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 16–78 Chain B; UniProt 16–78 Not recorded UV excision repair protein RAD23 homolog A × 1 (P54725) ASN-PRO-LEU-GLU-PHE-LEU × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.1M Tris, pH 7.5, 10% PEG 4000 Resolution 2.34 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 16–78 Chain D; UniProt 16–78 Not recorded UV excision repair protein RAD23 homolog A × 1 (P54725) ASN-PRO-LEU-GLU-PHE-LEU × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.1M Tris, pH 7.5, 10% PEG 4000 Resolution 2.34 Å R-free 0.220

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.

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

View Construct and Data Evidence
UniProt name VPR_HV1N5
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–64; UniProt 16–78 Author chain B; PDBConstruct 2–64; UniProt 16–78 Author chain C; PDBConstruct 2–64; UniProt 16–78 Author chain D; PDBConstruct 2–64; UniProt 16–78

UV excision repair protein RAD23 homolog A

Homo sapiens

UniProt P54725

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 319–358 Not recorded Protein Vpr × 2 (P12520) ASN-PRO-LEU-GLU-PHE-LEU × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.1M Tris, pH 7.5, 10% PEG 4000 Resolution 2.34 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 319–358 Not recorded Protein Vpr × 2 (P12520) ASN-PRO-LEU-GLU-PHE-LEU × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.1M Tris, pH 7.5, 10% PEG 4000 Resolution 2.34 Å R-free 0.220

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.

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

View Construct and Data Evidence
UniProt name RD23A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–40; UniProt 319–358 Author chain G; PDBConstruct 1–40; UniProt 319–358

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 6xqi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xqi
Deposition date deposition_date2020-07-09
Structure title titleStructure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
Keywords keywordsHIV, viral accessory protein, hHR23A, human, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.57
Radius of gyration Rg (electron density) rg_electron22.63
Forward intensity I(0) i026130500.00
Molecular weight molecular_weight40463.0 kDa
Excluded volume excluded_volume51104 ų
Envelope volume envelope_volume61490 ų
Hydration-shell volume shell_volume23303 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg28.91
Envelope Rg envelope_rg22.90
Shape Rg shape_rg22.64
Total Rg total_rg23.42
Total atoms total_atoms2859
Residues n_residues343
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 dmax84.9
Rg (real space) rg_real23.61
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real2.6130e+07
I(0) uncertainty (real space) i0_real_error3.8920e+05
Rg (reciprocal space) rg_reciprocal23.60
I(0) (reciprocal space) i0_reciprocal26130000.0000
Solution quality estimate total_estimate0.8424
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.436
Kurtosis Kurtosis kurtosis-0.083
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5435000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.689; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)