4AY9
Structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor
- PDB DOI: https://doi.org/10.2210/pdb4AY9/pdb
- Classification: HORMONE/RECEPTOR
- Organism(s): Homo sapiens
- Expression System: Homo sapiens
- Mutation(s): No 
- Deposited: 2012-06-19 Released: 2012-08-08 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.269 
- R-Value Work: 0.235 
- R-Value Observed: 0.237 
This is version 1.3 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
GLYCOPROTEIN HORMONES, ALPHA POLYPEPTIDE | A, C [auth D], E [auth G] | 92 | Homo sapiens | Mutation(s): 0  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01215 (Homo sapiens) Explore P01215  Go to UniProtKB:  P01215 | |||||
PHAROS:  P01215 GTEx:  ENSG00000135346  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01215 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
FOLLITROPIN SUBUNIT BETA | B, D [auth E], F [auth H] | 111 | Homo sapiens | Mutation(s): 0  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01225 (Homo sapiens) Explore P01225  Go to UniProtKB:  P01225 | |||||
PHAROS:  P01225 GTEx:  ENSG00000131808  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01225 | ||||
Sequence AnnotationsExpand | |||||
|
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
FOLLICLE-STIMULATING HORMONE RECEPTOR | G [auth X], H [auth Y], I [auth Z] | 350 | Homo sapiens | Mutation(s): 0  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P23945 (Homo sapiens) Explore P23945  Go to UniProtKB:  P23945 | |||||
PHAROS:  P23945 GTEx:  ENSG00000170820  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P23945 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
Ligands 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | J [auth A] K [auth A] L [auth B] M [auth B] N [auth D] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |
Modified Residues 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Type | Formula | 2D Diagram | Parent |
TYS Query on TYS | G [auth X], H [auth Y], I [auth Z] | L-PEPTIDE LINKING | C9 H11 N O6 S | TYR |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.269 
- R-Value Work: 0.235 
- R-Value Observed: 0.237 
- Space Group: P 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 70.716 | α = 60.3 |
b = 95.478 | β = 80.02 |
c = 95.675 | γ = 75.35 |
Software Name | Purpose |
---|---|
REFMAC | refinement |
HKL-3000 | data reduction |
XSCALE | data scaling |
PHASER | phasing |
Entry History 
Deposition Data
Revision History (Full details and data files)
- Version 1.0: 2012-08-08
Type: Initial release - Version 1.1: 2012-08-15
Changes: Database references - Version 1.2: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary - Version 1.3: 2023-12-20
Changes: Data collection, Database references, Refinement description, Structure summary