Structure of URAT1 in complex with benzbromarone. Determined by electron microscopy at 3.0 Å resolution. Released 18 Jun 2025.
Explore 9DKA in 3D Show helices and sheets RCSB PDB PDBe
9DKA contains 33 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 | 3-10 | 8 | |
| α-helix | 15-36 | 22 | |
| α-helix | 38-41 | 4 | |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 50 | 1 | |
| α-helix | 52-55 | 4 | |
| α-helix | 57-62 | 6 | |
| α-helix | 69-73 | 5 | |
| α-helix | 78 | 1 | |
| β-strand | 79-80 | 2 | 2 |
| β-strand | 84-85 | 2 | 2 |
| β-strand | 89-91 | 3 | 3 |
| α-helix | 110-112 | 3 | |
| β-strand | 113-115 | 3 | 3 |
| β-strand | 120-122 | 3 | 1 |
| β-strand | 129 | 1 | 4 |
| α-helix | 131-135 | 5 | |
| α-helix | 139-141 | 3 | |
| α-helix | 144-170 | 27 | |
| α-helix | 172-191 | 20 | |
| α-helix | 196-223 | 28 | |
| α-helix | 230-252 | 23 | |
| β-strand | 257 | 1 | 4 |
| α-helix | 258-266 | 9 | |
| α-helix | 268-275 | 8 | |
| α-helix | 283-289 | 7 | |
| α-helix | 292-306 | 15 | |
| α-helix | 309-314 | 6 | |
| α-helix | 317-323 | 7 | |
| α-helix | 325-329 | 5 | |
| α-helix | 333-336 | 4 | |
| α-helix | 337-342 | 6 | |
| α-helix | 344-367 | 24 | |
| α-helix | 372-374 | 3 | |
| α-helix | 378-402 | 25 | |
| α-helix | 405-423 | 19 | |
| α-helix | 431-459 | 29 | |
| α-helix | 465-485 | 21 | |
| α-helix | 486-492 | 7 | |
| α-helix | 495-512 | 18 | |
| α-helix | 516-517 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| URAT1 | A | protein | 518 | Homo sapiens | Q96S37 (AlphaFold model) |
>9DKA_1 URAT1 (chains A) MAFSELLDQVGGLGRFQVLQTVALVVPIMWLCTQSMLENFSAAVPSHRCWVPLLDNSTAQ ASVPGALGPEALLAVSIPPGPNQGPHQCRRFRQPQWQLLDPNATATNWSEAATEPCVDGW VYDRSTFTSTIVAKWDLVCDSQALKPMAQSIYLAGILVGAAVCGPASDRFGRRLVLTWSY LQMAVSGTAAAFAPTFPVYCLFRFLVAFAVAGVMMNTGTLVMEWTSAQARPLVMTLNSLG FSFGHVLMAAVAYGVRDWALLQLVVSVPFFLCFVYSCWLAESARWLLITGRLDRGLRELQ RVAAINGKRAVGDTLTPQVLLSAMQEELSVGQAPASLGTLLRTPGLRLRTCISTLCWFAF GFTFFGLALDLQALGSNIFLLQVLIGVVDIPAKIGTLLLLSRLGRRPTQAASLVLAGLCI LANTLVPHEMGALRSALAVLGLGGLGAAFTCITIYSGELFPTVLRMTAVGLGQMAARGGA ILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPET
| 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 basis of the urate transporter URAT1 inhibition by gout drugs. Suo, Y., Fedor, J.G., Zhang, H. et al. Nat Commun (2025) 16:5178-5178. DOI 10.1038/s41467-025-60480-3 · 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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