Structure of human URAT1 bound with benzbromarone. Determined by electron microscopy at 3.0 Å resolution. Released 15 Jan 2025.
Explore 9IRX in 3D Show helices and sheets RCSB PDB PDBe
9IRX contains 28 α-helices and 4 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 | 4-10 | 7 | |
| α-helix | 15-36 | 22 | |
| α-helix | 38-41 | 4 | |
| α-helix | 43-46 | 4 | |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 69-76 | 8 | |
| β-strand | 90-91 | 2 | 2 |
| β-strand | 113-114 | 2 | 2 |
| β-strand | 120-122 | 3 | 1 |
| α-helix | 131-135 | 5 | |
| α-helix | 139-141 | 3 | |
| α-helix | 144-169 | 26 | |
| α-helix | 172-191 | 20 | |
| α-helix | 196-222 | 27 | |
| α-helix | 227-229 | 3 | |
| α-helix | 230-254 | 25 | |
| α-helix | 258-266 | 9 | |
| α-helix | 268-275 | 8 | |
| α-helix | 276-278 | 3 | |
| α-helix | 280-282 | 3 | |
| α-helix | 283-289 | 7 | |
| α-helix | 292-304 | 13 | |
| α-helix | 317-323 | 7 | |
| α-helix | 337-342 | 6 | |
| α-helix | 347-367 | 21 | |
| α-helix | 378-402 | 25 | |
| α-helix | 406-425 | 20 | |
| α-helix | 431-455 | 25 | |
| α-helix | 465-485 | 21 | |
| α-helix | 486-491 | 6 | |
| α-helix | 495-511 | 17 | |
| α-helix | 512-514 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Solute carrier family 22 member 12 | A | protein | 553 | Homo sapiens | Q96S37 (AlphaFold model) |
>9IRX_1 Solute carrier family 22 member 12 (chains A) MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQ ASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGW VYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAVCGPASDRFGRRLVLTWSY LQMAVSGTAAAFAPTFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTSARARPLVMTLNSLG FSFGHGLTAAVAYGVRDWTLLQLAVSVPFFLCFLYSWWLAESARWLLTTGRLDRGLQELR RVAAINGKRAVQDTLTPEVLLSAMREELSVGQAPASLGTLLRTPGLRLRTCISTLCWFAF GFTFFGLALDLQALGSNIFLLQVLIGVVDIPAKMGALLLLSRLGRRPTLAASLLLAGLCI 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 |
Mechanisms of urate transport and uricosuric drugs inhibition in human URAT1. Guo, W., Wei, M., Li, Y. et al. Nat Commun (2025) 16:1512-1512. DOI 10.1038/s41467-025-56843-5 · 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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