9HPG: PDB entry 9HPG

The NTD dimer and the interfacing LBD region of the AMPAR complex GluA3(R439G,R163I)- TARP gamma2 in the apo state. Determined by electron microscopy at 3.35 Å resolution. Released 30 Jul 2025.

Method: Electron microscopy
Resolution: 3.35 Å
Organism: Rattus norvegicus
Chains: 2
Atoms: 6,947
Mol. weight: 265.24 kDa
Released: 30 Jul 2025

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

Secondary structure: helices and β-sheets

9HPG contains 33 α-helices and 50 β-strands across 2 chains. 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 B: 14 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	1
β-strand	9-11	3	2
β-strand	12	1	3
α-helix	18-31	14
β-strand	42-45	4	1
β-strand	49	1	3
α-helix	56-68	13
β-strand	73-75	3	2
α-helix	79-81	3
α-helix	82-92	11
β-strand	96-98	3	2
α-helix	101-103	3
β-strand	111-112	2	2
α-helix	115-116	2
α-helix	118-127	10
β-strand	133-137	5	4
α-helix	144-156	13
β-strand	160-164	5	4
α-helix	171-183	13
β-strand	188-192	5	4
α-helix	195-208	14
β-strand	216-219	4	4
α-helix	230-235	6
β-strand	238-243	6	4
α-helix	250-259	10
α-helix	277-298	22
α-helix	323-329	7
β-strand	337	1	5
β-strand	340	1	5
β-strand	344	1	6
β-strand	349	1	2
β-strand	350	1	6
β-strand	355-360	6	4
β-strand	365-372	8	4
β-strand	376-379	4	4

Chain C: 19 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	7
α-helix	17-32	16
β-strand	42-49	8	7
α-helix	55-68	14
β-strand	72-75	4	7
α-helix	79-92	14
β-strand	95-98	4	7
α-helix	101-103	3
β-strand	111-112	2	7
α-helix	118-128	11
β-strand	134-137	4	8
α-helix	144-156	13
β-strand	161-164	4	8
α-helix	171-183	13
β-strand	188-192	5	8
α-helix	195-208	14
β-strand	216-222	7	8
α-helix	224-226	3
α-helix	230-235	6
β-strand	238-243	6	8
α-helix	250-259	10
α-helix	277-298	22
α-helix	318-320	3
α-helix	323-330	8
β-strand	335-337	3	9
β-strand	340-342	3	9
β-strand	344	1	10
β-strand	349	1	7
β-strand	350	1	10
β-strand	354-360	7	8
β-strand	367-372	6	8
β-strand	378	1	8
β-strand	398-401	4	11
β-strand	404	1	12
β-strand	408	1	12
β-strand	409-410	2	13
α-helix	420-422	3
β-strand	423-424	2	13
α-helix	426-438	13
β-strand	443-446	4	11
β-strand	455	1	14
β-strand	462	1	14
α-helix	464-470	7
β-strand	476-477	2	11
α-helix	485-488	4
β-strand	492-493	2	11
β-strand	739-740	2	11
α-helix	747-759	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform Flip of Glutamate receptor 3,Voltage-dependent calcium channel gamma-2 subunit	B, C	protein	1179	Rattus norvegicus	P19492 (AlphaFold model), Q71RJ2 (AlphaFold model)

Sequence of entity 1 (B, C), FASTA

>9HPG_1 Isoform Flip of Glutamate receptor 3,Voltage-dependent calcium channel gamma-2 subunit (chains B, C)
GDYKDDDDKFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDS
SNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQ
MRPALKGAILSLLSYYKWEKFVYLYDTERGFSVLQAIMEAAVQNNWQVTAISVGNIKDVQ
EFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERV
MHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEA
FRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTN
YTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSSSSENRTIVVTTILESPYVMYKK
NHEQLEGNERYEGYCVDLAYEIAKHVGIKYKLSIVGDGKYGARDPETKIWNGMVGELVYG
RADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIV
FAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQG
CDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYG
TLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTM
NEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALGTPVNLAVLKLSEQGILDKLKNKWWY
DKGECGAKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLT
KNTQNFKPAPAGGSGSGGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKS
VSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRAS
SIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDP
SKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAIT
RIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTP
TATYNSDRDNSFLQVHNCIQKDSKDSLHANTANRRTTPV

Primary citation

Architecture, dynamics and biogenesis of GluA3 AMPA glutamate receptors. Pokharna, A., Stockwell, I., Ivica, J. et al. Nature (2025) 645:535-543. DOI 10.1038/s41586-025-09325-z · PubMed

Other PDB entries of the same protein (UniProt P19492 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4F29 1.75 Å, Quisqualate bound to the ligand binding domain of GluA3i
3LSW 1.75 Å, Aniracetam bound to the ligand binding domain of GluA3
4F1Y 1.79 Å, CNQX bound to the ligand binding domain of GluA3
3M3K 1.79 Å, Ligand binding domain (S1S2) of GluA3 (flop)
4F3B 1.82 Å, Glutamate bound to the D655A mutant of the ligand binding domain of GluA3
4F39 1.83 Å, Kainate bound to the ligand binding domain of GluA3
3DLN 1.91 Å, Crystal structure of the binding domain of the AMPA subunit GluR3 bound to glutamate
4F2O 1.91 Å, Quisqualate bound to the D655A mutant of the ligand binding domain of GluA3
6FPJ 1.96 Å, Structure of the AMPAR GluA3 N-terminal domain bound to phosphate
3LSX 2.01 Å, Piracetam bound to the ligand binding domain of GluA3
4F22 2.06 Å, Kainate bound to the K660A mutant of the ligand binding domain of GluA3
4F3G 2.06 Å, Kainate bound to the ligand binding domain of GluA3i

Browse structure collections

About this viewer

MolViewer shows 9HPG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.