9ogu

HIV-1 Env BG505 SOSIP.664-dPG-His in complex with PGT122 and 3BNC117 Fabs

Method: ELECTRON MICROSCOPY Dmax: 159.8 Å Quality: GOOD

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

HIV-1 Envelope Glycoprotein BG505 SOSIP.664 gp120

Human immunodeficiency virus 1

UniProt Q2N0S6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 18 其他Polymer 26 PDB declaration: 18-meric(18) Consistent with protein copy count Chain A; UniProt 30–505 Chain C; UniProt 30–505 Chain E; UniProt 30–505 Fragment:UNP residues 30-505 Mutation:T332N, A501C Envelope glycoprotein gp160 × 3 (A0A6H1VYE9) 3BNC117 Fab heavy chain × 3 3BNC117 Fab light chain × 3 PGT122 Fab heavy chain × 3 PGT122 Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 11 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

186 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S6_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 36–511; UniProt 30–505 Author chain C; PDBConstruct 36–511; UniProt 30–505 Author chain E; PDBConstruct 36–511; UniProt 30–505

Envelope glycoprotein gp160

Human immunodeficiency virus 1

UniProt A0A6H1VYE9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 18 其他Polymer 26 PDB declaration: 18-meric(18) Consistent with protein copy count Chain B; UniProt 509–661 Chain D; UniProt 509–661 Chain F; UniProt 509–661 Mutation:K567P, L568G HIV-1 Envelope Glycoprotein BG505 SOSIP.664 gp120 × 3 (Q2N0S6) 3BNC117 Fab heavy chain × 3 3BNC117 Fab light chain × 3 PGT122 Fab heavy chain × 3 PGT122 Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 11 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 A0A6H1VYE9_9PLVG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–152; UniProt 509–661 Author chain D; PDBConstruct 1–152; UniProt 509–661 Author chain F; PDBConstruct 1–152; UniProt 509–661

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 9ogu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ogu
Deposition date deposition_date2025-05-01
Structure title titleHIV-1 Env BG505 SOSIP.664-dPG-His in complex with PGT122 and 3BNC117 Fabs
Keywords keywords;broadly neutralizing antibody, gp140, vaccine design, stabilizing mutations, protein design, VIRAL PROTEIN, VIRAL PROTEIN-Immune System complex ;; VIRAL PROTEIN/Immune System
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.52
Radius of gyration Rg (electron density) rg_electron51.11
Forward intensity I(0) i01974080000.00
Molecular weight molecular_weight364740.0 kDa
Excluded volume excluded_volume453730 ų
Envelope volume envelope_volume656070 ų
Hydration-shell volume shell_volume104840 ų
Envelope diameter envelope_diameter160.6
Shell Rg shell_rg56.23
Envelope Rg envelope_rg50.33
Shape Rg shape_rg51.12
Total Rg total_rg51.21
Total atoms total_atoms25622
Residues n_residues2969
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 dmax159.8
Rg (real space) rg_real51.30
Rg uncertainty (real space) rg_real_error1.38
I(0) (real space) i0_real1.9740e+09
I(0) uncertainty (real space) i0_real_error3.4600e+07
Rg (reciprocal space) rg_reciprocal51.69
I(0) (reciprocal space) i0_reciprocal1975000000.0000
Solution quality estimate total_estimate0.8789
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.0
Skewness Skewness skewness0.108
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.680

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)