6u0n

Asymmetrically open conformational state (Class II) of HIV-1 Env trimer BG505 SOSIP.664 in complex with sCD4 and E51 Fab

Method: ELECTRON MICROSCOPY Dmax: 154.7 Å Quality: GOOD

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

Envelope glycoprotein 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 × 15 其他Polymer 5 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 32–505 Chain B; UniProt 32–505 Chain C; UniProt 32–505 Chain X; UniProt 509–661 Chain Y; UniProt 509–661 Chain Z; UniProt 509–661 Not recorded T-cell surface glycoprotein CD4 × 3 (P01730) E51 Fab heavy chain × 3 E51 Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-2)-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 ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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, 5
Chains and sequence ranges Author chain A; PDBConstruct 1–474; UniProt 32–505 Author chain B; PDBConstruct 1–474; UniProt 32–505 Author chain C; PDBConstruct 1–474; UniProt 32–505 Author chain X; PDBConstruct 1–153; UniProt 509–661 Author chain Y; PDBConstruct 1–153; UniProt 509–661 Author chain Z; PDBConstruct 1–153; UniProt 509–661

T-cell surface glycoprotein CD4

Homo sapiens

UniProt P01730

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 × 15 其他Polymer 5 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 26–207 Chain E; UniProt 26–207 Chain F; UniProt 26–207 Not recorded Envelope glycoprotein gp120 × 3 (Q2N0S6) E51 Fab heavy chain × 3 E51 Fab light chain × 3 Envelope glycoprotein gp41 × 3 (Q2N0S6) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-2)-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 ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

78 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–182; UniProt 26–207 Author chain E; PDBConstruct 1–182; UniProt 26–207 Author chain F; PDBConstruct 1–182; UniProt 26–207

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 6u0n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6u0n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6u0n
Deposition date deposition_date2019-08-14
Structure title titleAsymmetrically open conformational state (Class II) of HIV-1 Env trimer BG505 SOSIP.664 in complex with sCD4 and E51 Fab
Keywords keywordsBG505 SOSIP.664, E51, sCD4, Env, Env open conformation, asymmetrically open Env, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.37
Radius of gyration Rg (electron density) rg_electron49.74
Forward intensity I(0) i01117570000.00
Molecular weight molecular_weight274850.0 kDa
Excluded volume excluded_volume342380 ų
Envelope volume envelope_volume508740 ų
Hydration-shell volume shell_volume83138 ų
Envelope diameter envelope_diameter158.3
Shell Rg shell_rg55.68
Envelope Rg envelope_rg48.33
Shape Rg shape_rg49.73
Total Rg total_rg49.94
Total atoms total_atoms19304
Residues n_residues2414
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 dmax154.7
Rg (real space) rg_real50.10
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real1.1180e+09
I(0) uncertainty (real space) i0_real_error1.8270e+07
Rg (reciprocal space) rg_reciprocal50.57
I(0) (reciprocal space) i0_reciprocal1118000000.0000
Solution quality estimate total_estimate0.8205
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.9
Skewness Skewness skewness-0.052
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52870000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6u0nA01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology40 — HIV Envelope Protein Gp120; Chain G
Homologous superfamily homologous superfamily20 — Human immunodeficiency virus 1, Gp160, envelope glycoprotein
Domain ID domain_id6u0nB01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology40 — HIV Envelope Protein Gp120; Chain G
Homologous superfamily homologous superfamily20 — Human immunodeficiency virus 1, Gp160, envelope glycoprotein
Domain ID domain_id6u0nC01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology40 — HIV Envelope Protein Gp120; Chain G
Homologous superfamily homologous superfamily20 — Human immunodeficiency virus 1, Gp160, envelope glycoprotein
Domain ID domain_id6u0nD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6u0nE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6u0nF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)