1ha0

HEMAGGLUTININ PRECURSOR HA0

Method: X-RAY DIFFRACTION Dmax: 134.6 Å Quality: REASONABLE

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

PROTEIN (HEMAGGLUTININ PRECURSOR)

Influenza A virus

UniProt P03437

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 × 3 其他Polymer 9 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 25–518 Fragment:HA1, HA2 Mutation:R329Q beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 alpha-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 × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.50 Resolution 2.80 Å R-free 0.302

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.

42 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_IAAIC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–494; UniProt 25–518

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 1ha0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ha0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ha0
Deposition date deposition_date1998-10-08
Structure title titleHEMAGGLUTININ PRECURSOR HA0
Keywords keywordsGLYCOPROTEIN, MEMBRANE-FUSION PRECURSOR, VIRUS/VIRAL PROTEIN, 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_guinier36.89
Radius of gyration Rg (electron density) rg_electron37.45
Forward intensity I(0) i055721100.00
Molecular weight molecular_weight57403.0 kDa
Excluded volume excluded_volume71016 ų
Envelope volume envelope_volume93479 ų
Hydration-shell volume shell_volume24885 ų
Envelope diameter envelope_diameter136.9
Shell Rg shell_rg35.79
Envelope Rg envelope_rg37.58
Shape Rg shape_rg37.46
Total Rg total_rg37.27
Total atoms total_atoms4033
Residues n_residues494
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 dmax134.6
Rg (real space) rg_real37.72
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real5.5720e+07
I(0) uncertainty (real space) i0_real_error1.0700e+06
Rg (reciprocal space) rg_reciprocal37.21
I(0) (reciprocal space) i0_reciprocal55690000.0000
Solution quality estimate total_estimate0.6685
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.630
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3793000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.271; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.052; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ha0a1
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_idd1ha0a2
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_id1ha0A01
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_id1ha0A02
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)