9IRY: Human URAT1

Structure of human URAT1 bound with verinurad. Determined by electron microscopy at 3.2 Å resolution. Released 15 Jan 2025.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,146
Mol. weight: 59.9 kDa
Ligands: A1AIJ
Released: 15 Jan 2025

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

Secondary structure: helices and β-sheets

9IRY contains 20 α-helices and 6 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: 20 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	16-36	21
α-helix	38-41	4
β-strand	49	1	1
α-helix	69-74	6
β-strand	90-91	2	2
β-strand	113-114	2	2
β-strand	120	1	1
β-strand	129	1	3
α-helix	131-135	5
α-helix	139-141	3
α-helix	144-169	26
α-helix	172-191	20
α-helix	196-223	28
α-helix	227-229	3
α-helix	230-254	25
β-strand	257	1	3
α-helix	258-276	19
α-helix	337-342	6
α-helix	346-367	22
α-helix	371-374	4
α-helix	378-403	26
α-helix	405-425	21
α-helix	431-459	29
α-helix	462-486	25
α-helix	487-491	5
α-helix	495-512	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Solute carrier family 22 member 12	A	protein	553	Homo sapiens	Q96S37 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9IRY_1 Solute carrier family 22 member 12 (chains A)
MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQ
ASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGW
VYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAVCGPASDRFGRRLVLTWSY
LQMAVSGTAAAFAPTFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTSARARPLVMTLNSLG
FSFGHGLTAAVAYGVRDWTLLQLAVSVPFFLCFLYSWWLAESARWLLTTGRLDRGLQELR
RVAAINGKRAVQDTLTPEVLLSAMREELSVGQAPASLGTLLRTPGLRLRTCISTLCWFAF
GFTFFGLALDLQALGSNIFLLQVLIGVVDIPAKMGALLLLSRLGRRPTLAASLLLAGLCI
LANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGA
ILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATH
GTLGNSVLKSTQF

Ligands and cofactors

ID	Name	Formula	Copies
A1AIJ	verinurad	C20 H16 N2 O2 S	1

Primary citation

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:

9RXO 1.2 Å, Structure of the PDZ2 domain from human PDZK1 (NHERF3) with the C-terminal residues…
9RXR 1.69 Å, Structure of the PDZ1 domain from human PDZK1 (NHERF3) with the C-terminal residues…
9RXS 2.0 Å, Structure of the PDZ4 domain from human PDZK1 (NHERF3) with the C-terminal residues…
9DKC 2.55 Å, Structure of URAT1 in complex with TD-3
9DK9 2.68 Å, Structure of URAT1 with no external ligand added
9B1G 2.7 Å, Human urate transporter 1 URAT1 in complex with dotinurad
9DKB 2.74 Å, Structure of URAT1 in complex with lesinurad
9B1F 2.9 Å, Human urate transporter 1 URAT1 in apo state
9B1H 2.9 Å, Human urate transporter 1 URAT1 in complex with lesinurad
8WJG 3.0 Å, Cryo-EM structure of URAT1(R477S)
9B1J 3.0 Å, Urate bound human URAT1 in the inward-facing state
9B1M 3.0 Å, Pyrazinoate bound human URAT1 in the inward-facing state (site1)

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