9UXQ: Local refinement of AKG bound OXGR1

Local refinement of AKG bound OXGR1. Determined by electron microscopy at 2.89 Å resolution. Released 27 May 2026.

Method: Electron microscopy
Resolution: 2.89 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,309
Mol. weight: 38.43 kDa
Ligands: AKG
Released: 27 May 2026

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

Secondary structure: helices and β-sheets

9UXQ contains 17 α-helices and 2 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 R: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	29-34	6
α-helix	36-60	25
α-helix	67-84	18
α-helix	86-94	9
α-helix	103-136	34
α-helix	142-145	4
α-helix	147-165	19
α-helix	166-170	5
β-strand	174-175	2	1
α-helix	181	1
β-strand	182-183	2	1
α-helix	192-203	12
α-helix	204-208	5
α-helix	209-224	16
α-helix	234-269	36
α-helix	274-292	19
α-helix	294-298	5
α-helix	299-304	6
α-helix	307-312	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
2-oxoglutarate receptor 1	R	protein	337	Homo sapiens	Q96P68 (AlphaFold model)

Sequence of entity 1 (R), FASTA

>9UXQ_1 2-oxoglutarate receptor 1 (chains R)
MNEPLDYLANASDFPDYAAAFGNCTDENIPLKMHYLPVIYGIIFLVGFPGNAVVISTYIF
KMRPWKSSTIIMLNLACTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFSFHFNLYSS
ILFLTCFSIFRYCVIIHPMSCFSIHKTRCAVVACAVVWIISLVAVIPMTFLITSTNRTNR
SACLDLTSSDELNTIKWYNLILTATTFCLPLVIVTLCYTTIIHTLTHGLQTDSCLKQKAR
RLTILLLLAFYVCFLPFHILRVIRIESRLLSISCSIENQIHEAYIVSRPLAALNTFGNLL
LYVVVSDNFQQAVCSTVRCKVSGNLEQAKKISYSNNP

Ligands and cofactors

ID	Name	Formula	Copies
AKG	2-oxoglutaric acid	C5 H6 O5	1

Primary citation

Molecular architecture of OXGR1 reveals an evolutionary conserved mechanisms for metabolite surveillance. Zhang, X., Lu, Y., He, X. et al. EMBO J (2026) 45:4931-4955. DOI 10.1038/s44318-026-00823-y · PubMed

Other PDB entries of the same protein (UniProt Q96P68 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9VUS 2.37 Å, The structure of akg bound OXGR1
9VMO 2.4 Å, Cryo-EM structure of the ITA-OXGR1-Gq complex
9VMP 2.5 Å, Cryo-EM structure of the A-1-OXGR1-Gq complex
9VMN 2.6 Å, Cryo-EM structure of the a-KG-OXGR1-Gq complex
9VV6 2.62 Å, The structure of ITN bound OXGR1
9M1U 2.64 Å, Cryo-EM structure of Succinic Acid bound OXGR1-Gq complex
9M1S 2.65 Å, Cryo-EM structure of Itaconic acid bound OXGR1-Gq complex
9M1R 2.66 Å, Cryo-EM structure of AKG bound OXGR1-Gq complex
9UXN 2.7 Å, Local refinement of Succinate bound OXGR1
9VO2 2.7 Å, Cryo-EM structure of the OXGR1(CA)-Gq complex
26XH 2.82 Å, Cryo-EM structure of Maleic Acid bound OXGR1-Gq complex
8YYX 2.84 Å, Cryo-EM structure of OXGR1 bound to leukotriene E4 and Gq proteins

Browse structure collections

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