9B1O: Solute carrier family 22 member 12

Pyrazinoate bound human URAT1 in the inward-facing state (site3). Determined by electron microscopy at 3.1 Å resolution. Released 18 Sept 2024.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,945
Mol. weight: 59.6 kDa
Ligands: VGL, NAG
Released: 18 Sept 2024

Explore 9B1O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9B1O contains 36 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: 36 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	4-10	7
α-helix	15-36	22
α-helix	37-39	3
β-strand	47-49	3	1
α-helix	52-55	4
α-helix	60-61	2
α-helix	66-73	8
β-strand	76	1	2
β-strand	82	1	2
β-strand	87-88	2	3
α-helix	93-95	3
α-helix	102-104	3
α-helix	107-109	3
β-strand	110-111	2	3
β-strand	117-119	3	1
β-strand	126	1	4
α-helix	128-132	5
α-helix	136-138	3
α-helix	141-167	27
α-helix	169-188	20
α-helix	193-219	27
α-helix	224-226	3
α-helix	227-251	25
β-strand	254	1	4
α-helix	255-263	9
α-helix	265-272	8
α-helix	277-279	3
α-helix	280-285	6
α-helix	289-303	15
α-helix	306-310	5
α-helix	313-319	7
α-helix	321-324	4
α-helix	325-328	4
α-helix	333-338	6
α-helix	342-363	22
α-helix	367-370	4
α-helix	374-383	10
α-helix	385-398	14
α-helix	401-418	18
α-helix	427-452	26
α-helix	458-481	24
α-helix	482-488	7
α-helix	491-508	18
α-helix	512-513	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Solute carrier family 22 member 12	A	protein	547	Homo sapiens	Q96S37 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9B1O_1 Solute carrier family 22 member 12 (chains A)
FSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAVST
SLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGWVYDRS
IFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSYLQMAV
MGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLGFSFGH
GLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLPESARWLIIKGKPDQALQELRKVARI
NGHKEAKNLTIEVLMSSVKEEVASAKEPRSVLDLFCVPGLRFRTCISTLCWFAFGFTFFG
LALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCILANTLV
PHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAARGGAILGPLV
RLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKATHGTLGNS
VLKSTQF

Ligands and cofactors

ID	Name	Formula	Copies
VGL	Pyrazine-2-carboxylic acid	C5 H4 N2 O2	1
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

Transport mechanism and structural pharmacology of human urate transporter URAT1. Dai, Y., Lee, C.H. Cell Res (2024) 34:776-787. DOI 10.1038/s41422-024-01023-1 · 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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