9cxu

Endo H-treated hemagglutinin A/Hong Kong/1/68

Method: ELECTRON MICROSCOPY Dmax: 140.3 Å Quality: GOOD

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

Hemagglutinin HA1 chain

Influenza A virus (strain A/Hong Kong/1/1968 H3N2)

UniProt Q91MA7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 17–344 Chain B; UniProt 345–524 Chain C; UniProt 17–344 Chain D; UniProt 345–524 Chain E; UniProt 17–344 Chain F; UniProt 345–524 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;TBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.30 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.

46 other PDB entries and 90 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I68A4
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 25–352; UniProt 17–344 Author chain C; PDBConstruct 25–352; UniProt 17–344 Author chain E; PDBConstruct 25–352; UniProt 17–344 Author chain B; PDBConstruct 1–180; UniProt 345–524 Author chain D; PDBConstruct 1–180; UniProt 345–524 Author chain F; PDBConstruct 1–180; UniProt 345–524

Hemagglutinin HA2 chain,Green fluorescent protein fusion

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–233 Chain D; UniProt 1–233 Chain F; UniProt 1–233 Not recorded Hemagglutinin HA1 chain × 3 (Q91MA7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;TBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.30 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 231–463; UniProt 1–233 Author chain D; PDBConstruct 231–463; UniProt 1–233 Author chain F; PDBConstruct 231–463; UniProt 1–233

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 9cxu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cxu
Deposition date deposition_date2024-07-31
Structure title titleEndo H-treated hemagglutinin A/Hong Kong/1/68
Keywords keywordshemagglutinin, glycoprotein, H3, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.38
Radius of gyration Rg (electron density) rg_electron40.80
Forward intensity I(0) i0431433000.00
Molecular weight molecular_weight163990.0 kDa
Excluded volume excluded_volume202720 ų
Envelope volume envelope_volume264770 ų
Hydration-shell volume shell_volume55799 ų
Envelope diameter envelope_diameter138.3
Shell Rg shell_rg44.47
Envelope Rg envelope_rg40.50
Shape Rg shape_rg40.81
Total Rg total_rg40.97
Total atoms total_atoms11529
Residues n_residues1446
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 dmax140.3
Rg (real space) rg_real41.58
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real4.3140e+08
I(0) uncertainty (real space) i0_real_error7.3360e+06
Rg (reciprocal space) rg_reciprocal41.38
I(0) (reciprocal space) i0_reciprocal431300000.0000
Solution quality estimate total_estimate0.7820
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.6
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44340000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)