4ay9

Structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor

Method: X-RAY DIFFRACTION

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

GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	FOLLITROPIN SUBUNIT BETA × 1 （P01225） FOLLICLE-STIMULATING HORMONE RECEPTOR × 1 （P23945） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	FOLLITROPIN SUBUNIT BETA × 1 （P01225） FOLLICLE-STIMULATING HORMONE RECEPTOR × 1 （P23945） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	FOLLITROPIN SUBUNIT BETA × 1 （P01225） FOLLICLE-STIMULATING HORMONE RECEPTOR × 1 （P23945） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q96QJ4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–92； UniProt 25–116 Author chain D； PDBConstruct 1–92； UniProt 25–116 Author chain G； PDBConstruct 1–92； UniProt 25–116

FOLLITROPIN SUBUNIT BETA

HOMO SAPIENS

UniProt P01225

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE × 1 （Q96QJ4） FOLLICLE-STIMULATING HORMONE RECEPTOR × 1 （P23945） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE × 1 （Q96QJ4） FOLLICLE-STIMULATING HORMONE RECEPTOR × 1 （P23945） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE × 1 （Q96QJ4） FOLLICLE-STIMULATING HORMONE RECEPTOR × 1 （P23945） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FSHB_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–111； UniProt 19–129 Author chain E； PDBConstruct 1–111； UniProt 19–129 Author chain H； PDBConstruct 1–111； UniProt 19–129

FOLLICLE-STIMULATING HORMONE RECEPTOR

HOMO SAPIENS

UniProt P23945

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE × 1 （Q96QJ4） FOLLITROPIN SUBUNIT BETA × 1 （P01225） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE × 1 （Q96QJ4） FOLLITROPIN SUBUNIT BETA × 1 （P01225） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE × 1 （Q96QJ4） FOLLITROPIN SUBUNIT BETA × 1 （P01225） 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FSHR_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain X； PDBConstruct 1–350； UniProt 17–366 Author chain Y； PDBConstruct 1–350； UniProt 17–366 Author chain Z； PDBConstruct 1–350； UniProt 17–366

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	4ay9
Deposition date deposition_date	2012-06-19
Structure title title	Structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
Keywords keywords	HORMONE-RECEPTOR COMPLEX, LEUCINE-RICH REPEATS, LRR, GPCR; HORMONE/RECEPTOR
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.

4ay9__assembly_1__model_1

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

Download this curve (.dat)

4ay9__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4ay9__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.20 Å
Rg (electron density)	24.23 Å
Total Rg	25.03 Å
Atom count	4045
Residues	502
Excluded volume	71844 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4ay9__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4ay9__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`4ay9__assembly_3__model_1`	trimeric （3）	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 (5)

Entity 1 Entity 1 polymer

Description description	GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE
Molecular weight formula_weight	10183.8 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,G
Atom count atom_count	12344

APDVQDCPECTLQENPLFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	HOMO SAPIENS

Entity 2 Entity 2 polymer

Description description	FOLLITROPIN SUBUNIT BETA
Molecular weight formula_weight	12500.2 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,E,H

NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	HOMO SAPIENS

Entity 3 Entity 3 polymer

Description description	FOLLICLE-STIMULATING HORMONE RECEPTOR
Molecular weight formula_weight	40065.4 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X,Y,Z

GCHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNSAFNGTQLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILR

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	HOMO SAPIENS

Entity 4 Entity 4 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	15

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	223

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6. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d4ay9a_
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	d4ay9b_
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	d4ay9d_
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	d4ay9e_
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	d4ay9g_
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	d4ay9h_
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

CATH v4.4 (9 domains)

Domain ID domain_id	4ay9A00
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	4ay9B00
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	4ay9D00
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	4ay9E00
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	4ay9G00
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	4ay9H00
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	4ay9X00
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily	10 — Ribonuclease Inhibitor

Domain ID domain_id	4ay9Y00
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily	10 — Ribonuclease Inhibitor

Domain ID domain_id	4ay9Z00
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily	10 — Ribonuclease Inhibitor

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Unit-cell length a length_a	70.716 Å
Unit-cell length b length_b	95.478 Å
Unit-cell length c length_c	95.675 Å
Unit-cell angle α angle_alpha	60.30 °
Unit-cell angle β angle_beta	80.02 °
Unit-cell angle γ angle_gamma	75.35 °
Molecules per unit cell Z z_pdb	3

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

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	47.900 Å
R factor r_factor	0.2368
R_work r_work	0.2351
R_free r_free	0.2690

Structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor

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

GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE

State in the Current Structure

Other States of the Same Protein in the Database

FOLLITROPIN SUBUNIT BETA

State in the Current Structure

Other States of the Same Protein in the Database

FOLLICLE-STIMULATING HORMONE RECEPTOR

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

4ay9__assembly_1__model_1

4ay9__assembly_1__model_1 | I(q)

4ay9__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (6 domains)

CATH v4.4 (9 domains)

7. Citations (1)

Structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor

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

GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FOLLITROPIN SUBUNIT BETA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FOLLICLE-STIMULATING HORMONE RECEPTOR

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

4ay9__assembly_1__model_1

4ay9__assembly_1__model_1 | I(q)

4ay9__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (6 domains)

CATH v4.4 (9 domains)

7. Citations (1)