9JE0: Human URAT1

Human URAT1 bound to benzbromarone. Determined by electron microscopy at 3.23 Å resolution. Released 16 Oct 2024.

Method
Electron microscopy
Resolution
3.23 Å
Organism
Homo sapiens
Chains
1
Atoms
3,321
Mol. weight
60.1 kDa
Ligands
R75
Released
16 Oct 2024

Explore 9JE0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 27 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix21-4121
β-strand47-4931
α-helix52-554
α-helix58-603
α-helix69-768
β-strand7912
α-helix81-833
β-strand8512
α-helix861
β-strand90-9123
α-helix96-983
α-helix1041
α-helix110-1123
β-strand113-11423
β-strand120-12231
β-strand12914
α-helix131-1344
α-helix139-1413
α-helix144-17027
α-helix172-19019
α-helix196-22429
α-helix230-25425
β-strand25714
α-helix258-27215
α-helix273-2753
α-helix277-2815
α-helix340-3423
α-helix347-36721
α-helix371-3744
α-helix378-40225
α-helix406-42520
α-helix431-45929
α-helix468-48619
α-helix487-4915
α-helix496-51217

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Solute carrier family 22 member 12Aprotein553Homo sapiensQ96S37 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9JE0_1 Solute carrier family 22 member 12 (chains A)
MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQ
ASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGW
VYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSY
LQMAVMGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLG
FSFGHGLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLAESARWLLTTGRLDWGLQELW
RVAAINGKGAVQDTLTPEVLLSAMREELSMGQPPASLGTLLRMPGLRFRTCISTLCWFAF
GFTFFGLALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCI
LANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGA
ILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATH
GTLGNSVLKSTQF

Ligands and cofactors

IDNameFormulaCopies
R75[3,5-bis(bromanyl)-4-oxidanyl-phenyl]-(2-ethyl-1-benzofuran-3-yl)methanoneC17 H12 Br2 O31

Primary citation

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:

Browse structure collections

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