SAXSdb — 1htm

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

HEMAGGLUTININ HA1 CHAIN

uncultured beta proteobacterium UMTRA-608

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 6	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HEMA_IAAIC
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–27； UniProt 17–43 Author chain C； PDBConstruct 1–27； UniProt 17–43 Author chain E； PDBConstruct 1–27； UniProt 17–43 Author chain B； PDBConstruct 1–138； UniProt 383–520 Author chain D； PDBConstruct 1–138； UniProt 383–520 Author chain F； PDBConstruct 1–138； UniProt 383–520

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1htm
Deposition date deposition_date	1994-11-02
Structure title title	STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION
Keywords keywords	INFLUENZA VIRUS HEMAGGLUTININ, Viral protein; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1htm__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1htm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1htm__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	28.24 Å
Rg (electron density)	28.56 Å
Total Rg	28.95 Å
Atom count	3092
Residues	379
Excluded volume	54336 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1htm__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	HEMAGGLUTININ HA1 CHAIN
Molecular weight formula_weight	2776.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E
Atom count atom_count	3129

QDLPGNDNSTATLCLGHHAVPNGTLVK

Source Source

Source organism organism	uncultured beta proteobacterium UMTRA-608
NCBI taxonomy ID ncbi_taxonomy_id	140147

Entity 2 Entity 2 polymer

Description description	HEMAGGLUTININ HA2 CHAIN
Molecular weight formula_weight	16268.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F

LKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEEMGNGCFKIYHKCDNACIESIRNGTYDHDVYRDEALNNRFQIKG

Source Source

Source organism organism	uncultured beta proteobacterium UMTRA-608
NCBI taxonomy ID ncbi_taxonomy_id	140147

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	37

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1htmb_
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.1 — Influenza hemagglutinin (stalk)
Family Family family	h.3.1.1 — Influenza hemagglutinin (stalk)

Domain ID domain_id	d1htmd_
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.1 — Influenza hemagglutinin (stalk)
Family Family family	h.3.1.1 — Influenza hemagglutinin (stalk)

Domain ID domain_id	d1htmf_
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.1 — Influenza hemagglutinin (stalk)
Family Family family	h.3.1.1 — Influenza hemagglutinin (stalk)

CATH v4.4 (3 domains)

Domain ID domain_id	1htmB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1htmD00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1htmF00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily	10 —

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7. Citations (7)

Structure of influenza haemagglutinin at the pH of membrane fusion.

Nature (1994)

PMID: 8072525 · DOI: 10.1038/371037a0 PRIMARY

Crystals of a Fragment of Influenza Haemagglutinin in the Low Ph Induced Conformation

J.Mol.Biol. (1994)

Refinement of the Influenza Virus Hemagglutinin by Simulated Annealing

J.Mol.Biol. (1990)

Studies on the Structure of the Influenza Virus Haemagglutinin at the Ph of Membrane Fusion

J.Gen.Virol. (1988)

Analyses of the Antigenicity of Influenza Haemagglutinin at the Ph Optimum for Virus-Mediated Membrane Fusion

J.Gen.Virol. (1983)

Changes in the Conformation of Influenza Virus Hemagglutinin at the Ph Optimum of Virus-Mediated Membrane Fusion

Proc.Natl.Acad.Sci.USA (1982)

Structure of the Haemagglutinin Membrane Glycoprotein of Influenza Virus at 3 Angstroms Resolution

Nature (1981)

Unit-cell length a length_a	168.700 Å
Unit-cell length b length_b	231.700 Å
Unit-cell length c length_c	53.800 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.2220
R_work r_work	0.2220
R_free r_free	0.2910

STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

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

HEMAGGLUTININ HA1 CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1htm__assembly_1__model_1

1htm__assembly_1__model_1 | I(q)

1htm__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (7)

STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

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

HEMAGGLUTININ HA1 CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1htm__assembly_1__model_1

1htm__assembly_1__model_1 | I(q)

1htm__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (7)