4we4

The crystal structure of hemagglutinin from 1968 H3N2 influenza virus

Method: X-RAY DIFFRACTION Dmax: 132.5 Å Quality: REASONABLE

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

Hemagglutinin HA1 chain

Influenza A virus

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 Other combination Homooligomer Protein × 6 其他Polymer 12 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 25–345 Chain B; UniProt 346–517 Fragment:unp residues 25-345 Fragment:unp residues 346-517 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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 ;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 ; × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 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 × 6 PEG DI(HYDROXYETHYL)ETHER × 21 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.9;293 K;0.1M Tris-HCl, 25% PEG1000 Resolution 2.35 Å R-free 0.236

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 1–321; UniProt 25–345 Author chain B; PDBConstruct 1–172; UniProt 346–517

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 4we4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4we4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4we4
Deposition date deposition_date2014-09-09
Structure title titleThe crystal structure of hemagglutinin from 1968 H3N2 influenza virus
Keywords keywordsHemagglutinin, H3, influenza virus, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.16
Radius of gyration Rg (electron density) rg_electron37.62
Forward intensity I(0) i059751200.00
Molecular weight molecular_weight59651.0 kDa
Excluded volume excluded_volume73915 ų
Envelope volume envelope_volume99396 ų
Hydration-shell volume shell_volume26028 ų
Envelope diameter envelope_diameter138.9
Shell Rg shell_rg36.02
Envelope Rg envelope_rg37.88
Shape Rg shape_rg37.65
Total Rg total_rg37.40
Total atoms total_atoms4184
Residues n_residues493
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 dmax132.5
Rg (real space) rg_real38.00
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real5.9750e+07
I(0) uncertainty (real space) i0_real_error1.1150e+06
Rg (reciprocal space) rg_reciprocal37.48
I(0) (reciprocal space) i0_reciprocal59720000.0000
Solution quality estimate total_estimate0.6686
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.631
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4573000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.337; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.080; Smooth: 0.595

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4we4a_
Class classb — All beta proteins
Fold Fold foldb.19 — Viral protein domain
Superfamily Superfamily superfamilyb.19.1 — Viral protein domain
Family Family familyb.19.1.2 — Influenza hemagglutinin headpiece
Domain ID domain_idd4we4b_
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.1 — Influenza hemagglutinin (stalk)
Family Family familyh.3.1.1 — Influenza hemagglutinin (stalk)

CATH v4.4 (2 domains)

Domain ID domain_id4we4A01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology209 — Hemagglutinin (Ha1 Chain); Chain: A; domain 1
Homologous superfamily homologous superfamily20 — Haemagglutinin, alpha/beta domain, HA1 chain
Domain ID domain_id4we4B00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)