Crystal structure of recombinant human follicle stimulating hormone in complex with an anti-FSH alpha Fab. Determined by X-ray diffraction at 2.29 Å resolution. Released 11 Mar 2026.
Explore 9YXD in 3D Show helices and sheets RCSB PDB PDBe
9YXD contains 32 α-helices and 71 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8 | 1 | |
| β-strand | 9 | 1 | 1 |
| α-helix | 10 | 1 | |
| β-strand | 11-14 | 4 | 1 |
| α-helix | 16-18 | 3 | |
| β-strand | 20 | 1 | 2 |
| β-strand | 23 | 1 | 2 |
| α-helix | 24-25 | 2 | |
| β-strand | 26-38 | 13 | 1 |
| α-helix | 39-40 | 2 | |
| α-helix | 41-44 | 4 | |
| β-strand | 53-57 | 5 | 1 |
| β-strand | 59-70 | 12 | 3 |
| β-strand | 74-85 | 12 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-14 | 11 | 1 |
| α-helix | 15-17 | 3 | |
| β-strand | 19-35 | 17 | 1 |
| α-helix | 47-48 | 2 | |
| β-strand | 49-63 | 15 | 4 |
| β-strand | 66 | 1 | 5 |
| β-strand | 69 | 1 | 5 |
| β-strand | 72-86 | 15 | 4 |
| β-strand | 92-95 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-14 | 5 | 7 |
| β-strand | 19-25 | 7 | 6 |
| α-helix | 26-27 | 2 | |
| β-strand | 35-42 | 8 | 7 |
| β-strand | 49-53 | 5 | 7 |
| β-strand | 57-58 | 2 | 7 |
| α-helix | 59 | 1 | |
| β-strand | 66-70 | 5 | 6 |
| β-strand | 74-79 | 6 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 7 |
| β-strand | 101-104 | 4 | 7 |
| β-strand | 108-113 | 6 | 7 |
| β-strand | 117 | 1 | 8 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 9 |
| α-helix | 125-127 | 3 | |
| α-helix | 128-132 | 5 | |
| β-strand | 135-145 | 11 | 9 |
| β-strand | 146 | 1 | 8 |
| β-strand | 150-156 | 7 | 10 |
| β-strand | 159-160 | 2 | 10 |
| α-helix | 161 | 1 | |
| β-strand | 165-169 | 5 | 9 |
| α-helix | 170-173 | 4 | |
| β-strand | 179-188 | 10 | 9 |
| α-helix | 189-193 | 5 | |
| β-strand | 197-204 | 8 | 10 |
| β-strand | 211-216 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 11 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 12 |
| β-strand | 18-24 | 7 | 11 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 45-51 | 7 | 12 |
| β-strand | 58-60 | 3 | 12 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 11 |
| β-strand | 78-83 | 6 | 11 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 12 |
| β-strand | 103-107 | 5 | 12 |
| β-strand | 111-115 | 5 | 12 |
| β-strand | 121 | 1 | 13 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 14 |
| α-helix | 132-134 | 3 | |
| β-strand | 135-136 | 2 | 14 |
| β-strand | 139-149 | 11 | 14 |
| β-strand | 150 | 1 | 13 |
| β-strand | 155-158 | 4 | 15 |
| α-helix | 159-161 | 3 | |
| β-strand | 163 | 1 | 15 |
| β-strand | 167-169 | 3 | 14 |
| α-helix | 170-172 | 3 | |
| β-strand | 173-174 | 2 | 14 |
| β-strand | 180-189 | 10 | 14 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-204 | 6 | 15 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 16 |
| β-strand | 10-12 | 3 | 17 |
| β-strand | 18-25 | 8 | 16 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 17 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-51 | 6 | 17 |
| β-strand | 58-60 | 3 | 17 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 16 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 16 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 17 |
| β-strand | 110-111 | 2 | 17 |
| β-strand | 112 | 1 | 16 |
| β-strand | 115-119 | 5 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycoprotein hormones alpha chain | A | protein | 92 | Homo sapiens | P01215 (AlphaFold model) |
| Follitropin subunit beta | B | protein | 111 | Homo sapiens | P01225 (AlphaFold model) |
| Fab light chain | C | protein | 220 | Mus musculus | |
| Fab heavy chain | D | protein | 225 | Mus musculus | |
| Ig-like domain-containing protein | K | protein | 127 | Lama glama |
>9YXD_1 Glycoprotein hormones alpha chain (chains A) APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCC VAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
>9YXD_2 Follitropin subunit beta (chains B) NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYET VRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE
>9YXD_3 Fab light chain (chains C) DIELTQSPDSLSVSLGQRATISCRASESVDSYGNSFMQWYQQKPGQPPKLLIYRASNLES GIPARFSGTGSRTDFTLTINPVEADDVATYYCQQSDEYPYMYTFGGGTKLEIKRTVAAPS VFIFPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYS LSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>9YXD_4 Fab heavy chain (chains D) QVQLQQSGAELVKPGASVKLSCKASDYTFTSYWMHWVKQRPGQGLEWIGEINPTNGRTYY NEKFKSKATLTVDKSSSTAYMQLSSLTSEDSAVYYCARRYGNSFDYWGQGTTVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
>9YXD_5 Ig-like domain-containing protein (chains K) HHHHHHQVQLQESGGGLVQPGGSLRLSCAASGRTISRYAMSWFRQAPGKEREFVAVARRS GDGAFYADSVQGRFTVSRDDAKNTVYLQMNSLKPEDTAVYYCAIDSDTFYSGSYDYWGQG TQVTVSS
| ID | Name | Formula | Copies |
|---|---|---|---|
| BTB | 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol | C8 H19 N O5 | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (GOL) are not listed.
Disulfide Bond Mapping of Follitropin Delta, a Recombinant Follicle Stimulating Hormone (rFSH), by X-Ray Crystallography. Kalson, D., Joseph, J.S., Nudelman, H. et al. Pharmaceuticals (Basel) (2026) 19. DOI 10.3390/ph19030380 · PubMed
Other PDB entries of the same protein (UniProt P01215 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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