9ebc

H5N1 HA in complex with HC-5 Fab

Method: ELECTRON MICROSCOPY Dmax: 165.8 Å Quality: GOOD

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

Hemagglutinin HA1

Influenza A virus

UniProt A0AAX6NNG0

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 17–333 Chain C; UniProt 17–333 Chain E; UniProt 17–333 Not recorded Hemagglutinin HA2 × 3 (Q6DQ18) HC-5 Fab heavy chain × 3 HC-5 Fab light chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0AAX6NNG0_9INFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–317; UniProt 17–333 Author chain C; PDBConstruct 1–317; UniProt 17–333 Author chain E; PDBConstruct 1–317; UniProt 17–333

Hemagglutinin HA2

Influenza A virus

UniProt Q6DQ18

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 352–500 Chain D; UniProt 352–500 Chain F; UniProt 352–500 Fragment:UNP residues 345-506 Hemagglutinin HA1 × 3 (A0AAX6NNG0) HC-5 Fab heavy chain × 3 HC-5 Fab light chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I02A6
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–149; UniProt 352–500 Author chain D; PDBConstruct 1–149; UniProt 352–500 Author chain F; PDBConstruct 1–149; UniProt 352–500

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 9ebc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ebc
Deposition date deposition_date2024-11-12
Structure title titleH5N1 HA in complex with HC-5 Fab
Keywords keywordsComplex, Viral, Antibody, Monoclonal, 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_guinier48.35
Radius of gyration Rg (electron density) rg_electron48.01
Forward intensity I(0) i0849654000.00
Molecular weight molecular_weight237810.0 kDa
Excluded volume excluded_volume295950 ų
Envelope volume envelope_volume390580 ų
Hydration-shell volume shell_volume70415 ų
Envelope diameter envelope_diameter162.4
Shell Rg shell_rg48.24
Envelope Rg envelope_rg48.37
Shape Rg shape_rg48.00
Total Rg total_rg48.05
Total atoms total_atoms16740
Residues n_residues2115
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 dmax165.8
Rg (real space) rg_real48.37
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real8.4970e+08
I(0) uncertainty (real space) i0_real_error1.6070e+07
Rg (reciprocal space) rg_reciprocal48.35
I(0) (reciprocal space) i0_reciprocal849600000.0000
Solution quality estimate total_estimate0.8911
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.2
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.522
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70310000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.941

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)