8P3Q: Glutamate receptor 2

Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3. Determined by electron microscopy at 2.95 Å resolution. Released 30 Aug 2023.

Method: Electron microscopy
Resolution: 2.95 Å
Organism: Rattus norvegicus
Chains: 8
Atoms: 18,047
Mol. weight: 546.41 kDa
Ligands: POV, OLC, PLM
Released: 30 Aug 2023

Explore 8P3Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8P3Q contains 110 α-helices and 112 β-strands across 8 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 A: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	394	1
β-strand	395-399	5	1
β-strand	402	1	2
β-strand	406	1	2
β-strand	407-408	2	3
α-helix	412-414	3
α-helix	417-420	4
β-strand	421-422	2	3
α-helix	424-436	13
β-strand	440-444	5	1
α-helix	462-468	7
β-strand	474-475	2	1
β-strand	480-481	2	4
α-helix	483-486	4
β-strand	489-491	3	1
α-helix	492	1
α-helix	494	1
β-strand	496-498	3	4
β-strand	500	1	5
β-strand	502-505	4	6
α-helix	509-513	5
α-helix	516-518	3
β-strand	521	1	7
α-helix	523-545	23
α-helix	548-550	3
α-helix	576-584	9
α-helix	596-628	33
α-helix	636-640	5
β-strand	646-648	3	6
β-strand	650	1	8
α-helix	654-660	7
α-helix	665-675	11
β-strand	683	1	8
α-helix	686-696	11
β-strand	700-702	3	6
β-strand	705	1	5
α-helix	706-713	8
β-strand	720-723	4	6
β-strand	730-732	3	4
β-strand	735-737	3	1
α-helix	743-756	14
α-helix	758-764	7
α-helix	765-769	5
α-helix	786	1
β-strand	787	1	9
α-helix	788	1
α-helix	789-819	31

Chain B: 19 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	394-399	6	10
β-strand	402	1	11
β-strand	406	1	11
β-strand	407-408	2	12
α-helix	412-414	3
α-helix	417-420	4
β-strand	421-422	2	12
α-helix	424-436	13
β-strand	439-444	6	10
β-strand	453	1	13
β-strand	460	1	13
α-helix	462-468	7
β-strand	474	1	10
β-strand	475	1	14
β-strand	480	1	15
α-helix	483-486	4
β-strand	489-491	3	14
β-strand	497-498	2	16
β-strand	500-505	6	17
α-helix	516-518	3
β-strand	521	1	18
α-helix	523-545	23
α-helix	573-584	12
α-helix	596-623	28
α-helix	636-641	6
β-strand	646-648	3	17
β-strand	650	1	19
α-helix	654-661	8
α-helix	665-676	12
β-strand	683	1	19
α-helix	686-696	11
β-strand	700-705	6	17
α-helix	706-713	8
β-strand	720-723	4	17
β-strand	730-731	2	16
β-strand	732	1	15
β-strand	735-737	3	14
α-helix	743-756	14
α-helix	758-767	10
α-helix	785-786	2
β-strand	787	1	7
α-helix	789-791	3
α-helix	793-821	29

Chain C: 22 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	394-399	6	20
β-strand	401-402	2	21
β-strand	406	1	21
β-strand	407-408	2	22
α-helix	412-414	3
α-helix	417-420	4
β-strand	421-422	2	22
α-helix	424-436	13
β-strand	439-444	6	20
β-strand	453	1	23
β-strand	460	1	23
α-helix	462-468	7
β-strand	474	1	20
β-strand	475	1	24
β-strand	480	1	24
α-helix	483-486	4
β-strand	489-498	10	24
β-strand	500	1	25
β-strand	502-505	4	26
α-helix	511-513	3
α-helix	516-518	3
β-strand	521	1	27
α-helix	523-545	23
α-helix	548-550	3
α-helix	573-584	12
α-helix	596-623	28
α-helix	636-640	5
β-strand	646-648	3	26
β-strand	650	1	28
α-helix	654-661	8
α-helix	665-676	12
β-strand	683	1	28
α-helix	686-695	10
β-strand	700-702	3	26
β-strand	705	1	25
α-helix	706-713	8
β-strand	720-723	4	26
β-strand	730-737	8	24
α-helix	743-756	14
α-helix	758-764	7
α-helix	765-769	5
α-helix	786	1
β-strand	787	1	18
α-helix	788	1
α-helix	789-819	31

Chain D: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	394	1
β-strand	395-399	5	29
β-strand	402	1	30
β-strand	406	1	30
β-strand	407-408	2	31
α-helix	412-414	3
α-helix	417-420	4
β-strand	421-422	2	31
α-helix	424-436	13
β-strand	440-444	5	29
β-strand	453	1	32
β-strand	460	1	32
α-helix	462-468	7
β-strand	474-475	2	29
β-strand	480	1	29
α-helix	483-486	4
β-strand	489-498	10	29
β-strand	500-505	6	33
α-helix	506-509	4
α-helix	511-513	3
α-helix	516-518	3
β-strand	521	1	9
α-helix	523-544	22
α-helix	573-584	12
α-helix	596-625	30
α-helix	636-640	5
β-strand	646-648	3	33
β-strand	650	1	34
α-helix	654-661	8
α-helix	665-675	11
β-strand	683	1	34
α-helix	686-696	11
β-strand	700-705	6	33
α-helix	706-713	8
β-strand	720-723	4	33
β-strand	730-737	8	29
α-helix	743-755	13
α-helix	758-764	7
α-helix	765-769	5
α-helix	786	1
β-strand	787	1	27
α-helix	788	1
α-helix	789-822	34

Chain E: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-29	22
β-strand	34-38	5	35
β-strand	57-61	5	35
β-strand	65-68	4	35
β-strand	78-79	2	35
α-helix	93-103	11
α-helix	106-124	19
α-helix	134-160	27
β-strand	176	1	35
α-helix	178-209	32

Chain F: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-29	24
β-strand	34-35	2	36
β-strand	36-38	3	37
β-strand	57-59	3	37
β-strand	65-67	3	38
β-strand	68	1	37
β-strand	77-79	3	38
α-helix	93-103	11
α-helix	106-126	21
α-helix	134-159	26
β-strand	175-176	2	36
α-helix	178-208	31

Chain G: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-29	22
β-strand	34-38	5	39
β-strand	57-61	5	39
β-strand	65-67	3	39
β-strand	77-79	3	39
α-helix	80	1
α-helix	93-103	11
α-helix	106-126	21
α-helix	134-160	27
β-strand	174-176	3	39
α-helix	178-209	32

Chain H: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	6-29	24
β-strand	34-35	2	40
β-strand	36-38	3	41
β-strand	57-59	3	41
β-strand	65-66	2	42
β-strand	78-79	2	42
α-helix	94-103	10
α-helix	106-123	18
α-helix	133-160	28
β-strand	175-176	2	40
α-helix	178-209	32

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate receptor 2	A, B, C, D	protein	883	Rattus norvegicus	P19491 (AlphaFold model)
Voltage-dependent calcium channel gamma-2 subunit	E, F, G, H	protein	323	Rattus norvegicus	Q71RJ2 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8P3Q_1 Glutamate receptor 2 (chains A, B, C, D)
MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTP
HIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDG
THPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINV
GNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANL
GFTDGDLLKIQAGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALT
YDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNI
KFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTT
ILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKI
WNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLD
PLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWF
SLGAFMRQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDL
SKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGK
YAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRTPVNLAVLKLSEQGVL
DKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSR
AEAKRMKVAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI

Sequence of entity 2 (E, F, G, H), FASTA

>8P3Q_2 Voltage-dependent calcium channel gamma-2 subunit (chains E, F, G, H)
MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTH
SGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGL
CIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSF
YFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSS
SRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVH
NCIQKDSKDSLHANTANRRTTPV

Ligands and cofactors

ID	Name	Formula	Copies
POV	(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…	C42 H82 N O8 P	5
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	4
PLM	Palmitic acid	C16 H32 O2	7

Primary citation

Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor. Zhang, D., Ivica, J., Krieger, J.M. et al. Nature (2023) 621:877-882. DOI 10.1038/s41586-023-06528-0 · PubMed

Other PDB entries of the same protein (UniProt P19491 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YK4 1.0 Å, Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the…
5NG9 1.15 Å, Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist…
6YK5 1.15 Å, Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the…
6YK3 1.2 Å, Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the…
5JEI 1.23 Å, Crystal structure of the GluA2 LBD in complex with FW
4IGT 1.24 Å, Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist…
4YU0 1.26 Å, Crystal structure of a tetramer of GluA2 TR mutant ligand binding domains bound with…
5NIH 1.3 Å, Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist…
1MQI 1.35 Å, Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with…
5FTI 1.35 Å, Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (lithium form)
4U21 1.39 Å, GluA2flip sLBD complexed with FW and (R,R)-2b crystal form E
4FAT 1.4 Å, Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an…

Browse structure collections

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