Human URAT1 bound to benzbromarone. Determined by electron microscopy at 3.23 Å resolution. Released 16 Oct 2024.
Explore 9JE0 in 3D Show helices and sheets RCSB PDB PDBe
9JE0 contains 27 α-helices and 8 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 |
|---|---|---|---|
| α-helix | 21-41 | 21 | |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 52-55 | 4 | |
| α-helix | 58-60 | 3 | |
| α-helix | 69-76 | 8 | |
| β-strand | 79 | 1 | 2 |
| α-helix | 81-83 | 3 | |
| β-strand | 85 | 1 | 2 |
| α-helix | 86 | 1 | |
| β-strand | 90-91 | 2 | 3 |
| α-helix | 96-98 | 3 | |
| α-helix | 104 | 1 | |
| α-helix | 110-112 | 3 | |
| β-strand | 113-114 | 2 | 3 |
| β-strand | 120-122 | 3 | 1 |
| β-strand | 129 | 1 | 4 |
| α-helix | 131-134 | 4 | |
| α-helix | 139-141 | 3 | |
| α-helix | 144-170 | 27 | |
| α-helix | 172-190 | 19 | |
| α-helix | 196-224 | 29 | |
| α-helix | 230-254 | 25 | |
| β-strand | 257 | 1 | 4 |
| α-helix | 258-272 | 15 | |
| α-helix | 273-275 | 3 | |
| α-helix | 277-281 | 5 | |
| α-helix | 340-342 | 3 | |
| α-helix | 347-367 | 21 | |
| α-helix | 371-374 | 4 | |
| α-helix | 378-402 | 25 | |
| α-helix | 406-425 | 20 | |
| α-helix | 431-459 | 29 | |
| α-helix | 468-486 | 19 | |
| α-helix | 487-491 | 5 | |
| α-helix | 496-512 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Solute carrier family 22 member 12 | A | protein | 553 | Homo sapiens | Q96S37 (AlphaFold model) |
>9JE0_1 Solute carrier family 22 member 12 (chains A) MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQ ASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGW VYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSY LQMAVMGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLG FSFGHGLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLAESARWLLTTGRLDWGLQELW RVAAINGKGAVQDTLTPEVLLSAMREELSMGQPPASLGTLLRMPGLRFRTCISTLCWFAF GFTFFGLALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCI LANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGA ILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATH GTLGNSVLKSTQF
| ID | Name | Formula | Copies |
|---|---|---|---|
| R75 | [3,5-bis(bromanyl)-4-oxidanyl-phenyl]-(2-ethyl-1-benzofuran-3-yl)methanone | C17 H12 Br2 O3 | 1 |
Molecular mechanisms of urate transport by the native human URAT1 and its inhibition by anti-gout drugs. Wu, C., Zhang, C., Jin, S. et al. Cell Discov (2025) 11:33-33. DOI 10.1038/s41421-025-00779-z · PubMed
Other PDB entries of the same protein (UniProt Q96S37 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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