1qfw

TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV ANTI ALPHA SUBUNIT AND FV ANTI BETA SUBUNIT

Method: X-RAY DIFFRACTION

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

GONADOTROPIN ALPHA SUBUNIT

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	GONADOTROPHIN BETA SUBUNIT × 1 （P01233） ANTIBODY (ANTI ALPHA SUBUNIT) (LIGHT CHAIN) × 1 ANTIBODY (ANTI ALPHA SUBUNIT) (HEAVY CHAIN) × 1 ANTIBODY (ANTI BETA SUBUNIT) (LIGHT CHAIN) × 1 ANTIBODY (ANTI BETA SUBUNIT) (HEAVY CHAIN) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLHA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–92； UniProt 25–116

GONADOTROPHIN BETA SUBUNIT

OrganismNot specified

UniProt P01233

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	GONADOTROPIN ALPHA SUBUNIT × 1 （P01215） ANTIBODY (ANTI ALPHA SUBUNIT) (LIGHT CHAIN) × 1 ANTIBODY (ANTI ALPHA SUBUNIT) (HEAVY CHAIN) × 1 ANTIBODY (ANTI BETA SUBUNIT) (LIGHT CHAIN) × 1 ANTIBODY (ANTI BETA SUBUNIT) (HEAVY CHAIN) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CGHB_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–145； UniProt 1–145

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	1qfw
Deposition date deposition_date	1999-04-15
Structure title title	TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV ANTI ALPHA SUBUNIT AND FV ANTI BETA SUBUNIT
Keywords keywords	;GLYCOPROTEIN HORMONE, STIMULATION OF PRODUCTION OF PROGESTERONE, FVS SPECIFICALLY DIRECTED AGAINST ALPHA AND BETA SUBUNIT, IMMUNE SYSTEM ;; IMMUNE SYSTEM
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.

1qfw__assembly_1__model_1

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

Download this curve (.dat)

1qfw__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1qfw__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	36.53 Å
Rg (electron density)	36.83 Å
Total Rg	36.97 Å
Atom count	4938
Residues	651
Excluded volume	87033 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1qfw__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 (7)

Entity 1 Entity 1 polymer

Description description	GONADOTROPIN ALPHA SUBUNIT
Molecular weight formula_weight	10219.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4938

APDTQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS

Entity 2 Entity 2 polymer

Description description	GONADOTROPHIN BETA SUBUNIT
Molecular weight formula_weight	15549.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ

Entity 3 Entity 3 polymer

Description description	ANTIBODY (ANTI ALPHA SUBUNIT) (LIGHT CHAIN)
Molecular weight formula_weight	12688.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

DIELTQSPDSLAVSLGQRATISCRASESVDSYGNSFMQWYQQKPGQPPKLLIYRASNLESGIPARFSGTGSRTDFTLTINPVEADDVATYYCQQSDEYPYMYTFGGGTKLEIKR

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090

Entity 4 Entity 4 polymer

Description description	ANTIBODY (ANTI ALPHA SUBUNIT) (HEAVY CHAIN)
Molecular weight formula_weight	12896.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

QVQLQQSGAELVKPGASVKLSCKASDYTFTSYWMHWVKQRPGQGLEWIGEINPTNGRTYYNEKFKSKATLTVAASASTAAMQASSLTSEDSAVYYCARRYGNSFDYWGQGTTVTVSS

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090

Entity 5 Entity 5 polymer

Description description	ANTIBODY (ANTI BETA SUBUNIT) (LIGHT CHAIN)
Molecular weight formula_weight	11896.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M

DIELTQSPKSMSMSVGERVTLSCKASETVDSFVSWYQQKPEQSPKLLIFGASNRFSGVPDRFTGSGSATDFTLTISSVQAEDFADYHCGQTYNHPYTFGGGTKLEIKR

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090

Entity 6 Entity 6 polymer

Description description	ANTIBODY (ANTI BETA SUBUNIT) (HEAVY CHAIN)
Molecular weight formula_weight	13461.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

QVQLQESGGHLVKPGGSLKLSCAASGFAFSSFDMSWIRQTPEKRLEWVASITNVGTYTYYPGSVKGRFSISRDNARNTLNLQMSSLRSEDTALYFCARQGTAAQPYWYFDVWGAGTTVTVSS

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090

Entity 7 Entity 7 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1qfwa_
Class class	g — Small proteins
Fold Fold fold	g.17 — Cystine-knot cytokines
Superfamily Superfamily superfamily	g.17.1 — Cystine-knot cytokines
Family Family family	g.17.1.4 — Gonadodropin/Follitropin

Domain ID domain_id	d1qfwb_
Class class	g — Small proteins
Fold Fold fold	g.17 — Cystine-knot cytokines
Superfamily Superfamily superfamily	g.17.1 — Cystine-knot cytokines
Family Family family	g.17.1.4 — Gonadodropin/Follitropin

Domain ID domain_id	d1qfwh1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d1qfwh2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1qfwi1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d1qfwi2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1qfwl_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d1qfwm_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (6 domains)

Domain ID domain_id	1qfwA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	1qfwB00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	1qfwH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1qfwI00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1qfwL00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1qfwM00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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7. Citations (7)

;Crystal structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits. ;

J.Mol.Biol. (1999)

PMID: 10373373 · DOI: 10.1006/jmbi.1999.2845 PRIMARY

Partially deglycosylated human choriogonadotropin, stabilized by intersubunit disulfide bonds, shows full bioactivity.

Eur.J.Biochem. (1998)

PMID: 9578495 · DOI: 10.1046/j.1432-1327.1998.2530354.x

Crystal structure of human chorionic gonadotropin.

Nature (1994)

PMID: 8202136 · DOI: 10.1038/369455a0

Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein.

Structure (1994)

PMID: 7922031 · DOI: 10.1016/s0969-2126(00)00054-x

;Crystallization and characterization of human chorionic gonadotropin in chemically deglycosylated and enzymatically desialylated states. ;

Biochemistry (1989)

PMID: 2611225 · DOI: 10.1021/bi00450a001

Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction.

J.Biol.Chem. (1989)

PMID: 2536708

Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action.

J.Biol.Chem. (1975)

PMID: 172504

Unit-cell length a length_a	104.900 Å
Unit-cell length b length_b	104.900 Å
Unit-cell length c length_c	150.100 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	9.000 Å
R factor r_factor	0.2600
R_work r_work	0.2600
R_free r_free	0.3100

TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV ANTI ALPHA SUBUNIT AND FV ANTI BETA SUBUNIT

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

GONADOTROPIN ALPHA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

GONADOTROPHIN BETA SUBUNIT

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

1qfw__assembly_1__model_1

1qfw__assembly_1__model_1 | I(q)

1qfw__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

Source Source

Entity 6 Entity 6 polymer

Polymer Polymer

Source Source

Entity 7 Entity 7 non-polymer

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (8 domains)

CATH v4.4 (6 domains)

7. Citations (7)

TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV ANTI ALPHA SUBUNIT AND FV ANTI BETA SUBUNIT

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

GONADOTROPIN ALPHA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

GONADOTROPHIN BETA SUBUNIT

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

1qfw__assembly_1__model_1

1qfw__assembly_1__model_1 | I(q)

1qfw__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

Source Source

Entity 6 Entity 6 polymer

Polymer Polymer

Source Source

Entity 7 Entity 7 non-polymer

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (8 domains)

CATH v4.4 (6 domains)

7. Citations (7)