9JDY: Human URAT1

Human URAT1 bound with verinurad. 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: 3,312
Mol. weight: 60.02 kDa
Ligands: A1AIJ
Released: 16 Oct 2024

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

Secondary structure: helices and β-sheets

9JDY contains 23 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: 23 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	21-40	20
β-strand	47-49	3	1
α-helix	52-55	4
α-helix	69-76	8
β-strand	79	1	2
α-helix	81-83	3
α-helix	84	1
β-strand	85	1	2
α-helix	86	1
β-strand	90-91	2	3
α-helix	96-98	3
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	196-222	27
α-helix	230-254	25
β-strand	257	1	4
α-helix	258-274	17
α-helix	276-280	5
α-helix	350-367	18
α-helix	378-403	26
α-helix	406-425	20
α-helix	431-456	26
α-helix	468-486	19
α-helix	487-491	5
α-helix	496-512	17

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

>9JDY_1 Solute carrier family 22 member 12 (chains A)
MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQ
ASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGW
VYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSY
LQMAVMGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLG
FSFGHGLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLAESARWLLTTGRLDWGLQELW
RVAAINGKGAVQDTLTPEVLLSAMREELSMGQPPASLGTLLRMPGLRFRTCISTLCWFAF
GFTFFGLALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCI
LANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGA
ILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATH
GTLGNSVLKSTQF

Ligands and cofactors

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

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:

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)

Browse structure collections

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