7kl1

Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D)

Method: X-RAY DIFFRACTION D_max: 83.0 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 7–274	Mutation：D135N, Q223K	Glutamate receptor ionotropic, NMDA 2B × 1 （Q13224） EDO 1,2-ETHANEDIOL × 1 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 7–274	Mutation：D135N, Q223K	Glutamate receptor ionotropic, NMDA 2B × 1 （Q13224） EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7KL1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2VZ6 Structure of human calcium calmodulin dependent protein kinase type II alpha (CAMK2A) in complex with Indirubin E804 Deposited 2008-07-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 13–302（290 aa） Fragment：KINASE DOMAIN, RESIDUES 13-302	Not recorded	FEF (2Z,3E)-2,3'-BIINDOLE-2',3(1H,1'H)-DIONE 3-{O-[(3R)-3,4-DIHYDROXYBUTYL]OXIME} × 1 PGO S-1,2-PROPANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；12% PEG6000, 0.1M TRIS PH8.5	Resolution 2.30 Å R-free 0.203
2VZ6 Structure of human calcium calmodulin dependent protein kinase type II alpha (CAMK2A) in complex with Indirubin E804 Deposited 2008-07-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 13–302（290 aa） Fragment：KINASE DOMAIN, RESIDUES 13-302	Not recorded	FEF (2Z,3E)-2,3'-BIINDOLE-2',3(1H,1'H)-DIONE 3-{O-[(3R)-3,4-DIHYDROXYBUTYL]OXIME} × 1 PGO S-1,2-PROPANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；12% PEG6000, 0.1M TRIS PH8.5	Resolution 2.30 Å R-free 0.203
3SOA Full-length human CaMKII Deposited 2011-06-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–474（474 aa）	Mutation：K42M, D135N, T306V	DB8 4-[(2,4-dichloro-5-methoxyphenyl)amino]-6-methoxy-7-[3-(4-methylpiperazin-1-yl)propoxy]quinoline-3-carbonitrile × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；288.15 K；1.2 M Ammonium Tartrate, 100 mM bistrispropane, pH 5.5, VAPOR DIFFUSION, temperature 288.15K	Resolution 3.55 Å R-free 0.327
5IG3 Crystal structure of the human CaMKII-alpha hub Deposited 2016-02-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 345–475（131 aa） Fragment：UNP residues 345-475 Chain B 345–475（131 aa） Fragment：UNP residues 345-475 Chain C 345–475（131 aa） Fragment：UNP residues 345-475 Chain D 345–475（131 aa） Fragment：UNP residues 345-475 Chain E 345–475（131 aa） Fragment：UNP residues 345-475 Chain F 345–475（131 aa） Fragment：UNP residues 345-475	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；295 K；35 % (v/v) MPD, 0.1 M HEPES pH 7.3	Resolution 2.75 Å R-free 0.268
6OF8 Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CamKII-alpha hub domain Deposited 2019-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 345–475（131 aa） Chain B 345–475（131 aa） Chain C 345–475（131 aa） Chain D 345–475（131 aa） Chain E 345–475（131 aa） Chain F 345–475（131 aa） Chain G 345–475（131 aa）	Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M	K POTASSIUM ION × 10 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；17 mg/mL mutant hub in 25 mM Tris, 150 mM KCl, 10% (v/v) glycerol, 2 mM DTT, 1 mM TCEP, pH 8.0 was mixed 1:1 with 235 mM K3Citrate, 15% (w/v) PEG 3350, pH 8.0	Resolution 2.10 Å R-free 0.258
6VZK Crystal structure of human CaMKII-alpha (CAMK2A)kinase domain Deposited 2020-02-28	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	HC4 4'-HYDROXYCINNAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；PEG 6000, 50 mM HEPES, 3-Aminobenzene-sulfonic acid, 5-Sulfosalicylic acid dihydrate, p-Coumaric acid, PIPES, Terephthalic acid, Vanillic acid	Resolution 2.55 Å R-free 0.294
6W4O CaMKII alpha-30 Cryo-EM reconstruction Deposited 2020-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 13 PDB declaration: tridecameric	Chain A 7–478（472 aa） Chain B 7–478（472 aa） Chain C 7–478（472 aa） Chain D 7–478（472 aa） Chain E 7–478（472 aa） Chain F 7–478（472 aa） Chain G 7–478（472 aa） Chain I 7–478（472 aa） Chain J 7–478（472 aa） Chain K 7–478（472 aa） Chain L 7–478（472 aa） Chain M 7–478（472 aa） Chain O 7–478（472 aa）	Mutation：K37M	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
6W4P CaMKII alpha-30 Cryo-EM reconstruction - Class B Deposited 2020-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 13 PDB declaration: tridecameric	Chain A 7–478（472 aa） Chain B 7–478（472 aa） Chain C 7–478（472 aa） Chain D 7–478（472 aa） Chain E 7–478（472 aa） Chain F 7–478（472 aa） Chain G 7–478（472 aa） Chain H 7–478（472 aa） Chain I 7–478（472 aa） Chain J 7–478（472 aa） Chain K 7–478（472 aa） Chain L 7–478（472 aa） Chain M 7–478（472 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.60 Å
6X5G Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and LRRC7 inhibitory domain Deposited 2020-05-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	GOL GLYCEROL × 2 BCN BICINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；10% w/v PEG 20000, 2% v/v 1,4-Dioxane, 0.1 M Bicine	Resolution 1.85 Å R-free 0.227
6X5Q Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluA1 Deposited 2020-05-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1 M Tris, 28% w/v PEG 4000	Resolution 2.14 Å R-free 0.235
7KL0 Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2020-10-28	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258
7KL0 Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2020-10-28	Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 7–274（268 aa）	Mutation：D135N, Q223K	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258
7KL2 Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2020-10-28	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.15 M DL-Malic acid pH 7, 20% PEG 3350	Resolution 2.56 Å R-free 0.293
7REC Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CaMKII alpha hub bound to 5-HDC Deposited 2021-07-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 345–475（131 aa） Fragment：hub (UNP residues 345-475) Chain B 345–475（131 aa） Fragment：hub (UNP residues 345-475) Chain C 345–475（131 aa） Fragment：hub (UNP residues 345-475) Chain D 345–475（131 aa） Fragment：hub (UNP residues 345-475) Chain E 345–475（131 aa） Fragment：hub (UNP residues 345-475) Chain F 345–475（131 aa） Fragment：hub (UNP residues 345-475) Chain G 345–475（131 aa） Fragment：hub (UNP residues 345-475)	Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M Mutation：T354N, E355Q, T412N, I414M, I464H, F467M	7ZV 5-hydroxydiclofenac × 12 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.1；298 K；100 nL protein + compound in 25 mM Tris, 150 mM potassium chloride, 2 mM DTT, 1 mM TCEP, 10% v/v glycerol, pH 8.0, 10% DMSO + 100 nL well solution (200 mM potassium acetate, 20% w/v PEG3350, pH 8.1), equilibrated against 45 uL well solution	Resolution 2.20 Å R-free 0.244
7UIQ Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1 Deposited 2022-03-29	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M HEPES, 16% PEG 6000, 0.1% v/v Triton X-114	Resolution 3.11 Å R-free 0.309
7UIQ Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1 Deposited 2022-03-29	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 7–274（268 aa）	Mutation：D135N, Q223K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M HEPES, 16% PEG 6000, 0.1% v/v Triton X-114	Resolution 3.11 Å R-free 0.309
7UIR Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1 in complex with ATP Deposited 2022-03-29	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M HEPES, 16% PEG 6000, 0.1% v/v Triton X-114	Resolution 3.10 Å R-free 0.274
7UIR Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1 in complex with ATP Deposited 2022-03-29	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 7–274（268 aa）	Mutation：D135N, Q223K	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M HEPES, 16% PEG 6000, 0.1% v/v Triton X-114	Resolution 3.10 Å R-free 0.274
7UIS Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2022-03-29	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M Bis-tris propane pH 6.5, 0.2 M Sodium chloride, 25% PEG 3350	Resolution 2.58 Å R-free 0.268
7UJP Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.56 Å R-free 0.281
7UJP Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 7–274（268 aa）	Mutation：D135N, Q223K	MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.56 Å R-free 0.281
7UJQ Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.25 Å R-free 0.271
7UJQ Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 7–274（268 aa）	Mutation：D135N, Q223K	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.25 Å R-free 0.271
7UJR Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：Q223K	EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 3350, 5% Ethanol	Resolution 1.95 Å R-free 0.252
7UJS Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B in complex with ADP Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：Q223K	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 3350	Resolution 2.75 Å R-free 0.262
7UJT Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) in complex with ATP Deposited 2022-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–274（268 aa）	Mutation：D135N, Q223K	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.2 M Sodium chloride, 25% PEG 3350	Resolution 2.10 Å R-free 0.246
9EOY Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CaMKII alpha hub bound to PIPA Deposited 2024-03-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric	Chain A 345–475（131 aa） Chain B 345–475（131 aa） Chain C 345–475（131 aa） Chain D 345–475（131 aa） Chain E 345–475（131 aa） Chain F 345–475（131 aa） Chain G 345–475（131 aa）	Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M Mutation：T354N, E355Q, T412N, I414M, I464H, and F467M	ACT ACETATE ION × 12 A1H6K 2-[6-(4-chlorophenyl)imidazo[1,2-b]pyridazin-2-yl]ethanoic acid × 4 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293.15 K；500 nL protein + 2.65 mM compound in 25 mM Tris, 150 mM KCl, 10 mM imidazole, 1 mM DTT, 10% glycerol, pH 8.5, 10% DMSO + 1000 nL well solution (11% w/v PEG3350, 300 mM potassium acetate, pH 8.0), equilibrated against 50 uL well solution.	Resolution 2.10 Å R-free 0.251

21 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KCC2A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–268； UniProt 7–274 Author chain B； PDBConstruct 1–268； UniProt 7–274

Glutamate receptor ionotropic, NMDA 2B

OrganismNot specified

UniProt Q13224

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1289–1310	Mutation：S1303D	Calcium/calmodulin-dependent protein kinase type II subunit alpha × 1 （Q9UQM7） EDO 1,2-ETHANEDIOL × 1 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1289–1310	Mutation：S1303D	Calcium/calmodulin-dependent protein kinase type II subunit alpha × 1 （Q9UQM7） EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 7KL1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
10EX SK5A-Matured apo state in complex with GluN1-GluN2B, full refinement Deposited 2026-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 59–845（787 aa） Chain D 59–845（787 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.08 Å
10EY SK5B-Matured in complex with GluN1-GluN2B, full refinement Deposited 2026-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
10EZ SK3D-Germline in complex with GluN1-GluN2B, full refinement Deposited 2026-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.76 Å
10FD SK5G-Matured in complex with GluN1-GluN2B, full refinement Deposited 2026-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
10FE OX1-Germline in complex with GluN1-GluN2B, full refinement Deposited 2026-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.55 Å
10FF SK5A-Matured glycine/glutamate in complex with GluN1-GluN2B, full refinement Deposited 2026-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.06 Å
10FL SK5G-Germline Deposited 2026-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.81 Å
10FN SK5A-Germline in complex with GluN1-GluN2B, full refinement Deposited 2026-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.52 Å
10FO SK5B-Germline in complex with GluN1-GluN2B, full refinement Deposited 2026-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.46 Å
5EWJ CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH IFENPRODIL Deposited 2015-11-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 31–394（364 aa） Fragment：Amino Terminal Domain (UNP residues 31-394)	Mutation：N348D	NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 QEL 4-[(1R,2S)-2-(4-benzylpiperidin-1-yl)-1-hydroxypropyl]phenol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；3.6M Na Formate, 0.1 M Hepes pH 7.0	Resolution 2.77 Å R-free 0.211
5EWJ CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH IFENPRODIL Deposited 2015-11-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 31–394（364 aa） Fragment：Amino Terminal Domain (UNP residues 31-394)	Mutation：N348D	NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 QEL 4-[(1R,2S)-2-(4-benzylpiperidin-1-yl)-1-hydroxypropyl]phenol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；3.6M Na Formate, 0.1 M Hepes pH 7.0	Resolution 2.77 Å R-free 0.211
5EWL CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH MK-22 Deposited 2015-11-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 31–394（364 aa） Fragment：Amino Terminal Domain (UNP residues 31-394)	Mutation：N348D	NA SODIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 5SL ~{N}-[(1~{S},3~{S})-3-[3-[(4-methylphenyl)methyl]-1,2,4-oxadiazol-5-yl]cyclopentyl]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；3.6M Na Formate, 0.1 M Hepes pH 7.0	Resolution 2.98 Å R-free 0.217
5EWL CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH MK-22 Deposited 2015-11-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 31–394（364 aa） Fragment：Amino Terminal Domain (UNP residues 31-394)	Mutation：N348D	NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 5SL ~{N}-[(1~{S},3~{S})-3-[3-[(4-methylphenyl)methyl]-1,2,4-oxadiazol-5-yl]cyclopentyl]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；3.6M Na Formate, 0.1 M Hepes pH 7.0	Resolution 2.98 Å R-free 0.217
5EWM CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH EVT-101 Deposited 2015-11-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 31–394（364 aa） Fragment：Amino Terminal Domain (UNP residues 31-394)	Mutation：N348D	NA SODIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 5SM 5-[3-[bis(fluoranyl)methyl]-4-fluoranyl-phenyl]-3-[(2-methylimidazol-1-yl)methyl]pyridazine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；3.6M Na Formate, 0.1 M Hepes pH 7.0	Resolution 2.76 Å R-free 0.211
5EWM CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH EVT-101 Deposited 2015-11-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 31–394（364 aa） Fragment：Amino Terminal Domain (UNP residues 31-394)	Mutation：N348D	NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 5SM 5-[3-[bis(fluoranyl)methyl]-4-fluoranyl-phenyl]-3-[(2-methylimidazol-1-yl)methyl]pyridazine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；3.6M Na Formate, 0.1 M Hepes pH 7.0	Resolution 2.76 Å R-free 0.211
7EU8 Structure of the human GluN1-GluN2B NMDA receptor in complex with S-ketamine,glycine and glutamate Deposited 2021-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–842（842 aa） Chain D 1–842（842 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 JC9 (2~{S})-2-(2-chlorophenyl)-2-(methylamino)cyclohexan-1-one × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.07 Å
7KL0 Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2020-10-28	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1289–1310（22 aa）	Mutation：S1303D	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258
7KL0 Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2020-10-28	Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1289–1310（22 aa）	Mutation：S1303D	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 6000, 19mM HECAMEG	Resolution 2.40 Å R-free 0.258
7KL2 Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2020-10-28	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1289–1310（22 aa）	Mutation：S1303D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.15 M DL-Malic acid pH 7, 20% PEG 3350	Resolution 2.56 Å R-free 0.293
7UIS Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) Deposited 2022-03-29	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1289–1310（22 aa）	Mutation：S1303D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.1 M Bis-tris propane pH 6.5, 0.2 M Sodium chloride, 25% PEG 3350	Resolution 2.58 Å R-free 0.268
7UJP Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1289–1310（22 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.56 Å R-free 0.281
7UJP Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1289–1310（22 aa）	Not recorded	MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.56 Å R-free 0.281
7UJQ Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1289–1310（22 aa）	Not recorded	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.25 Å R-free 0.271
7UJQ Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1289–1310（22 aa）	Not recorded	UZD methyl 6-O-(heptylcarbamoyl)-beta-L-altropyranoside × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1 M Bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, 0.1 M Ammonium sulfate, 25% PEG 3350, 19mM Methyl 6-O-(N-heptylcarbamoyl)-alpha-D-glucopyranoside	Resolution 2.25 Å R-free 0.271
7UJR Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1289–1310（22 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 3350, 5% Ethanol	Resolution 1.95 Å R-free 0.252
7UJS Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B in complex with ADP Deposited 2022-03-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1289–1310（22 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 3350	Resolution 2.75 Å R-free 0.262
7UJT Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) in complex with ATP Deposited 2022-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1289–1310（22 aa）	Mutation：S1303D	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.2 M Sodium chloride, 25% PEG 3350	Resolution 2.10 Å R-free 0.246
8VUU Human GluN1-2B with Fab 007-168 Deposited 2024-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 31–845（815 aa） Chain D 31–845（815 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.05 Å
8VUV Human GluN1-2B with Fab 007-168 Local refinement of ATD Deposited 2024-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 31–387（357 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.69 Å
9D37 Nonactive state of Gly-,Glu- bound GluN1a-2B-2D NMDAR Deposited 2024-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa）	Mutation：C838S, C849S, C588S	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.34 Å
9D38 Open state of Gly-,Glu-,EU1622-240 bound GluN1a-2B-2D NMDAR Deposited 2024-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa）	Mutation：C588S, C838S, C849S	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.95 Å
9D39 Gly-,PPDA- bound GluN1a-2B-2D NMDAR Deposited 2024-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa）	Mutation：C588S, C838S, C849S	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 2JL (2S,3R)-1-(phenanthren-2-ylcarbonyl)piperazine-2,3-dicarboxylic acid × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9D3A Nonactive state of Gly-,Glu- bound GluN1a-2B-2D NMDAR (Low-res) Deposited 2024-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa）	Mutation：C838S, C849S	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.78 Å
9D3B Gly-,Glu-,(S)-DQP-997-74 bound GluN1a-2B-2D NMDAR Deposited 2024-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa）	Mutation：C588S, C838S, C849S	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GLU GLUTAMIC ACID × 2 A1A15 4-{(3R,5S)-5-(4-chlorophenyl)-3-[4-(4-chlorophenyl)-2-oxo-1,2-dihydroquinolin-3-yl]pyrazolidin-1-yl}-3,3-difluoro-4-oxobutanoic acid × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.71 Å
9D3C Gly-,Glu-,(S)-(+)-ketamine bound GluN1a-2B-2D NMDAR Deposited 2024-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa）	Mutation：S588C, C838S, C849S	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 GLU GLUTAMIC ACID × 2 JC9 (2~{S})-2-(2-chlorophenyl)-2-(methylamino)cyclohexan-1-one × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.96 Å
9IYP Structure of the human GluN1-N2B NMDA receptors in the Mg2+ bound state Deposited 2024-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 35–842（808 aa） Chain D 35–842（808 aa）	Not recorded	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 7RC (2R)-4-(3-phosphonopropyl)piperazine-2-carboxylic acid × 2 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.27 Å
9IYQ Structure of the human GluN1-N2B NMDA receptors in the Mg2+ free state Deposited 2024-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–842（842 aa） Chain D 1–842（842 aa）	Not recorded	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 7RC (2R)-4-(3-phosphonopropyl)piperazine-2-carboxylic acid × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
9OOQ Closed state of Gly/Glu/24S-HC bound hGluN1a-2B NMDAR Deposited 2025-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Mutation：C588S,C838S,C849S Mutation：C588S,C838S,C849S	GLY GLYCINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 GLU GLUTAMIC ACID × 2 A1CE1 24S-hydroxycholesterol × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9OOR Open state Gly/Glu/24S-HC bound hGluN1a-2B NMDAR Deposited 2025-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Mutation：C588S,C838S,C849S Mutation：C588S,C838S,C849S	GLY GLYCINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 GLU GLUTAMIC ACID × 2 A1CE1 24S-hydroxycholesterol × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å
9OOS Non-active state of Gly/Glu/Pregnenolone Sulfate bound hGluN1a-2B NMDAR Deposited 2025-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Mutation：C588S,C838S,C849S Mutation：C588S,C838S,C849S	GLY GLYCINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 GLU GLUTAMIC ACID × 2 A8W Pregnenolone sulfate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å
9OOT Pre-active state of Gly/Glu/Pregnenolone Sulfate bound hGluN1a-2B NMDAR Deposited 2025-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 27–852（826 aa） Chain D 27–852（826 aa）	Mutation：C588S,C838S,C849S Mutation：C588S,C838S,C849S	GLY GLYCINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 GLU GLUTAMIC ACID × 2 A8W Pregnenolone sulfate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.13 Å

35 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NMDE2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–22； UniProt 1289–1310 Author chain D； PDBConstruct 1–22； UniProt 1289–1310

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7kl1
Deposition date deposition_date	2020-10-28
Structure title title	Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D)
Keywords keywords	CaMKII, Kinase, Human, CAMK2A, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	25.14 Å
Radius of gyration Rg (electron density) rg_electron	24.29 Å
Forward intensity I(0) i0	69064400.00
Molecular weight molecular_weight	65076.0 kDa
Excluded volume excluded_volume	81506 Å³
Envelope volume envelope_volume	97233 Å³
Hydration-shell volume shell_volume	32657 Å³
Envelope diameter envelope_diameter	88.1 Å
Shell Rg shell_rg	32.16 Å
Envelope Rg envelope_rg	24.14 Å
Shape Rg shape_rg	24.29 Å
Total Rg total_rg	25.11 Å
Total atoms total_atoms	4592
Residues n_residues	564
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	83.0 Å
Rg (real space) rg_real	25.02 Å
Rg uncertainty (real space) rg_real_error	0.43 Å
I(0) (real space) i0_real	6.9060e+07
I(0) uncertainty (real space) i0_real_error	8.6580e+05
Rg (reciprocal space) rg_reciprocal	25.06 Å
I(0) (reciprocal space) i0_reciprocal	69070000.0000
Solution quality estimate total_estimate	0.8836
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	30.3 Å
Skewness Skewness skewness	0.221
Kurtosis Kurtosis kurtosis	-0.371
Angular range angular_range	— – 0.3150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	26180000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Calcium/calmodulin-dependent protein kinase type II subunit alpha
Molecular weight formula_weight	30548.1 kDa
EC 编号 ec_number	2.7.11.17
Mutation mutation	D135N, Q223K
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4718

TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHR

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Glutamate receptor ionotropic, NMDA 2B
Molecular weight formula_weight	2782.2 kDa
Mutation mutation	S1303D
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

KAQKKNRNKLRRQHDYDTFVDL

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	118

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8. Citations (1)

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Unit-cell length a length_a	72.893 Å
Unit-cell length b length_b	92.133 Å
Unit-cell length c length_c	91.338 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	48.500 Å
R factor r_factor	0.2084
R_work r_work	0.2060
R_free r_free	0.2575

fit	/app/data/saxs_computation/kl/7kl1/7kl1.fit
pddf	/app/data/pr_computation/kl/7kl1/7kl1.pr.out
profile	/app/data/saxs_computation/kl/7kl1/7kl1.dat

Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D)

1. Protein Identity and Related Structures Protein Identity & Related Structures

Calcium/calmodulin-dependent protein kinase type II subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

Glutamate receptor ionotropic, NMDA 2B

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)