9yxd

Crystal structure of recombinant human follicle stimulating hormone in complex with an anti-FSH alpha Fab

Method: X-RAY DIFFRACTION Dmax: 123.5 Å Quality: REASONABLE

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

Glycoprotein hormones alpha chain

Homo sapiens

UniProt P01215

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 Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 25–116 Not recorded Follitropin subunit beta × 1 (P01225) Fab light chain × 1 Fab heavy chain × 1 Ig-like domain-containing protein × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.05 M Calcium acetate, 0.1 M Bis-Tris pH 7, 30% v/v PEG 550 MME Resolution 2.29 Å R-free 0.235

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.

15 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

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

Follitropin subunit beta

Homo sapiens

UniProt P01225

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 Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 19–129 Not recorded Glycoprotein hormones alpha chain × 1 (P01215) Fab light chain × 1 Fab heavy chain × 1 Ig-like domain-containing protein × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;0.05 M Calcium acetate, 0.1 M Bis-Tris pH 7, 30% v/v PEG 550 MME Resolution 2.29 Å R-free 0.235

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.

5 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

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

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 9yxd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yxd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yxd
Deposition date deposition_date2025-10-27
最后修订 last_revision2026-03-11
Structure title titleCrystal structure of recombinant human follicle stimulating hormone in complex with an anti-FSH alpha Fab
Keywords keywordsGonadotropin, Glycoprotein hormone, cystine knot cytokine, GPCR signaling, HORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier36.34
Radius of gyration Rg (electron density) rg_electron36.42
Forward intensity I(0) i0113027000.00
Molecular weight molecular_weight82735.0 kDa
Excluded volume excluded_volume102400 ų
Envelope volume envelope_volume138680 ų
Hydration-shell volume shell_volume34751 ų
Envelope diameter envelope_diameter132.5
Shell Rg shell_rg39.26
Envelope Rg envelope_rg35.95
Shape Rg shape_rg36.35
Total Rg total_rg36.82
Total atoms total_atoms5827
Residues n_residues743
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 dmax123.5
Rg (real space) rg_real36.68
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real1.1300e+08
I(0) uncertainty (real space) i0_real_error2.2250e+06
Rg (reciprocal space) rg_reciprocal36.47
I(0) (reciprocal space) i0_reciprocal113000000.0000
Solution quality estimate total_estimate0.6044
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.503
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7501000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 0.028; Positv: 1.000; Valcen: 0.737; Smooth: 0.583

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)