Follicle stimulating hormone receptor. Determined by electron microscopy at 6.0 Å resolution. Released 22 Mar 2023.
Explore 8I2H in 3D Show helices and sheets RCSB PDB PDBe
8I2H contains 16 α-helices and 26 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 23-26 | 4 | 1 |
| β-strand | 29-33 | 5 | 1 |
| β-strand | 50-54 | 5 | 1 |
| β-strand | 60-61 | 2 | 2 |
| α-helix | 62 | 1 | |
| β-strand | 74-78 | 5 | 1 |
| β-strand | 85-86 | 2 | 2 |
| β-strand | 91-92 | 2 | 3 |
| β-strand | 99-102 | 4 | 1 |
| β-strand | 105 | 1 | 4 |
| β-strand | 110-111 | 2 | 2 |
| β-strand | 116-117 | 2 | 3 |
| β-strand | 124-128 | 5 | 1 |
| β-strand | 130 | 1 | 4 |
| β-strand | 143 | 1 | 5 |
| β-strand | 147-152 | 6 | 1 |
| β-strand | 159-160 | 2 | 6 |
| β-strand | 169 | 1 | 5 |
| β-strand | 173-176 | 4 | 1 |
| β-strand | 184-185 | 2 | 6 |
| β-strand | 194 | 1 | 7 |
| β-strand | 195-199 | 5 | 1 |
| α-helix | 211-214 | 4 | |
| β-strand | 218 | 1 | 7 |
| β-strand | 222-224 | 3 | 1 |
| β-strand | 243-245 | 3 | 1 |
| β-strand | 266-268 | 3 | 1 |
| α-helix | 272-286 | 15 | |
| β-strand | 345-347 | 3 | 1 |
| α-helix | 349-350 | 2 | |
| α-helix | 363-389 | 27 | |
| α-helix | 396-424 | 29 | |
| α-helix | 429-438 | 10 | |
| α-helix | 440-472 | 33 | |
| α-helix | 483-502 | 20 | |
| α-helix | 504-506 | 3 | |
| α-helix | 511-513 | 3 | |
| α-helix | 525-557 | 33 | |
| α-helix | 565-596 | 32 | |
| α-helix | 604-623 | 20 | |
| α-helix | 624-628 | 5 | |
| α-helix | 631-642 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Follicle-stimulating hormone receptor | A | protein | 682 | Homo sapiens | P23945 (AlphaFold model) |
>8I2H_1 Follicle-stimulating hormone receptor (chains A) LGSGCHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLE KIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIK HLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNCAFNGT QLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLK KLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSS LAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILRVLIWFIS ILAITGNIIVLVILTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYA IDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLDCKVQLRHAASVMVMG WIFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICGCYIHIY LTVRNPNIVSSSSDTRIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKAKILLVL FHPINSCANPFLYAIFTKNFRRDFFILLSKCGCYEMQAQIYRTETSSTVHNTHPRNGHCS SAPRVTNGSTYILVPLSHLAQN
Mechanism of hormone and allosteric agonist mediated activation of follicle stimulating hormone receptor. Duan, J., Xu, P., Zhang, H. et al. Nat Commun (2023) 14:519-519. DOI 10.1038/s41467-023-36170-3 · PubMed
Other PDB entries of the same protein (UniProt P23945 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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