8flw

Cryo-EM Structure of PGT145 DU303 Fab in complex with BG505 DS-SOSIP.664

Method: ELECTRON MICROSCOPY Dmax: 152.5 Å Quality: GOOD

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

Envelope glycoprotein gp41

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 × 8 其他Polymer 23 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 509–661 Chain B; UniProt 509–661 Chain C; UniProt 30–510 Chain F; UniProt 509–661 Chain G; UniProt 30–510 Chain I; UniProt 30–510 Fragment:UNP residues 509-661 Fragment:UNP residues 30-510 PGT145 DU303 Heavy × 1 PGT145 DU303 Light × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ;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 ; × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 35 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;PBS 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.

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 3, 4
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 509–661 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain F; PDBConstruct 1–153; UniProt 509–661 Author chain C; PDBConstruct 1–481; UniProt 30–510 Author chain G; PDBConstruct 1–481; UniProt 30–510 Author chain I; PDBConstruct 1–481; UniProt 30–510

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 8flw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8flw
Deposition date deposition_date2022-12-22
Structure title titleCryo-EM Structure of PGT145 DU303 Fab in complex with BG505 DS-SOSIP.664
Keywords keywordsCD4, HIV-1, SOSIP, Vaccine, IMMUNE SYSTEM, llama, V2 apex, therapeutic, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.91
Radius of gyration Rg (electron density) rg_electron45.38
Forward intensity I(0) i0895114000.00
Molecular weight molecular_weight241120.0 kDa
Excluded volume excluded_volume299360 ų
Envelope volume envelope_volume442110 ų
Hydration-shell volume shell_volume79785 ų
Envelope diameter envelope_diameter165.0
Shell Rg shell_rg51.40
Envelope Rg envelope_rg44.97
Shape Rg shape_rg45.39
Total Rg total_rg45.58
Total atoms total_atoms16868
Residues n_residues1939
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 dmax152.5
Rg (real space) rg_real45.78
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real8.9510e+08
I(0) uncertainty (real space) i0_real_error1.6090e+07
Rg (reciprocal space) rg_reciprocal45.91
I(0) (reciprocal space) i0_reciprocal895200000.0000
Solution quality estimate total_estimate0.8524
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.8
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.111
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha102000000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.706

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8flwL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)