9da9

Crystal structure of GluN1/GluN2A agonist-binding domains in complex with 7CKA and glutamate

Method: X-RAY DIFFRACTION D_max: 86.2 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1

Rattus norvegicus

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 394–800	Not recorded	Glutamate receptor ionotropic, NMDA 2A × 1 （Q00959） CKA 7-Chlorokynurenic acid × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M ammonium acetate and 14-18% PEG 4000	Resolution 2.05 Å R-free 0.228

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 9DA9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9PZS Native GluN1/GluN2A/GluN2B in complex with 5F11 and 3D2 Fabs (class 1), glycine and glutamate bound state Deposited 2025-08-11	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 × 10 PDB declaration: decameric	Chain A 1–938（938 aa） Chain C 1–938（938 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
9PZT Native GluN1/GluN2A in complex with 5F11 and 3D2 Fabs (class 3), glycine and glutamate-bound state Deposited 2025-08-11	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 × 12 PDB declaration: 12-meric	Chain A 1–938（938 aa） Chain C 1–938（938 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.14 Å
9PZU Native GluN1/GluN2B in complex with 5F11 Fab (class 4), glycine and glutamate-bound state Deposited 2025-08-11	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 × 8 PDB declaration: octameric	Chain A 1–938（938 aa） Chain C 1–938（938 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.36 Å
9PZV Native GluN1/GluN2A in complex with 5F11 and 3D2 Fabs, local ATD dimer Deposited 2025-08-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–938（938 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.92 Å
9UN2 native NMDAR receptor-GluN1/N2B in the inactive state Deposited 2025-04-23	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 A 26–844（819 aa） Chain C 26–844（819 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9UN3 native NMDA receptor-GluN1/N2B in the open state Deposited 2025-04-23	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 A 25–841（817 aa） Chain C 25–841（817 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.37 Å
9UNJ native NMDA receptor-GluN1/N2A-S1 in closed state Deposited 2025-04-23	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 A 25–837（813 aa） Chain C 25–837（813 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 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 3.93 Å
9UNK native NMDA receptor-GluN1/N2B in the closed state Deposited 2025-04-23	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 A 24–844（821 aa） Chain C 24–844（821 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 32 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 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 3.37 Å
9UNM native NMDA receptor-GluN1/N2A-S2 in the closed state Deposited 2025-04-23	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 A 27–837（811 aa） Chain C 27–837（811 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 11 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 6.37 Å
9UNN native NMDA receptor-GluN1/N2A-S3 in the closed state Deposited 2025-04-24	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 A 25–840（816 aa） Chain C 25–840（816 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 25 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 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 3.29 Å
9UNO native NMDA receptor-GluN1/N2A in the inactive state Deposited 2025-04-24	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 A 25–837（813 aa） Chain C 25–837（813 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 23 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.55 Å
9UNP native NMDA receptor-GluN1/N2A/N2B-S2 in the closed state Deposited 2025-04-24	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 A 24–844（821 aa） Chain C 24–844（821 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 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 3.27 Å
9UNQ native NMDA receptor-GluN1/N2A/2B in inactive state Deposited 2025-04-24	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 A 25–842（818 aa） Chain C 25–842（818 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9UNR native NMDA receptor-GluN1/N2A/N2B-S1 in the closed state Deposited 2025-04-24	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 A 25–843（819 aa） Chain C 25–843（819 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 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 2.98 Å

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NMDZ1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–292； UniProt 394–800

Glutamate receptor ionotropic, NMDA 2A

Rattus norvegicus

UniProt Q00959

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 B； UniProt 402–802	Not recorded	Glutamate receptor ionotropic, NMDA 1 × 1 （P35438） CKA 7-Chlorokynurenic acid × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M ammonium acetate and 14-18% PEG 4000	Resolution 2.05 Å R-free 0.228

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9DA9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2A5S Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate Deposited 2005-06-30	Different construct 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 401–539（139 aa） Fragment：S1S2 ligand-binding core	Not recorded	GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；277 K；PEG 8000, HEPES, calcium acetate, pH 7, EVAPORATION, temperature 277K	Resolution 1.70 Å R-free 0.223
2A5S Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate Deposited 2005-06-30	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 401–539（139 aa） Fragment：S1S2 ligand-binding core	Not recorded	GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；277 K；PEG 8000, HEPES, calcium acetate, pH 7, EVAPORATION, temperature 277K	Resolution 1.70 Å R-free 0.223
2A5T Crystal Structure Of The NR1/NR2A ligand-binding cores complex Deposited 2005-06-30	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 401–539（139 aa） Fragment：S1S2 ligand-binding core	Not recorded	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；277 K；PEG 8000, HEPES, Calcium acetate, pH 7., EVAPORATION, temperature 277K	Resolution 2.00 Å R-free 0.253
4NF4 Crystal structure of GluN1/GluN2A ligand-binding domain in complex with DCKA and glutamate Deposited 2013-10-30	Different construct 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 402–539（138 aa） Fragment：Ligand-binding domain; unp residues 402-539; unp residues 661-802 Chain B 661–802（142 aa） Fragment：Ligand-binding domain; unp residues 402-539; unp residues 661-802	Mutation：S758T Mutation：S758T	2JK 4-hydroxy-5,7-dimethylquinoline-2-carboxylic acid × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；300 K；PEG2000MME, HEPES, pH 7, VAPOR DIFFUSION, temperature 300K	Resolution 2.00 Å R-free 0.217
4NF5 Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and D-AP5 Deposited 2013-10-30	Different construct 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 402–539（138 aa） Fragment：unp residues 402-539; unp residues 661-802 Chain B 661–802（142 aa） Fragment：unp residues 402-539; unp residues 661-802	Mutation：S758T Mutation：S758T	GLY GLYCINE × 1 GOL GLYCEROL × 3 2JJ 5-phosphono-D-norvaline × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；300 K；PEG2000MME, HEPES, pH 7, VAPOR DIFFUSION, temperature 300K	Resolution 1.90 Å R-free 0.213
4NF6 Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and PPDA Deposited 2013-10-30	Different construct 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 402–539（138 aa） Fragment：Ligand-binding domain; unp residues 402-539; unp residues 661-802 Chain B 661–802（142 aa） Fragment：Ligand-binding domain; unp residues 402-539; unp residues 661-802	Mutation：S758T Mutation：S758T	GLY GLYCINE × 1 2JL (2S,3R)-1-(phenanthren-2-ylcarbonyl)piperazine-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；300 K；PEG2000MMG and HEPES, pH 7, VAPOR DIFFUSION, temperature 300K	Resolution 2.10 Å R-free 0.215
4NF8 Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and glutamate in PEG2000MME Deposited 2013-10-30	Different construct 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 402–539（138 aa） Fragment：Ligand-binding domain; unp residues 402-539; unp residues 661-802 Chain B 661–802（142 aa） Fragment：Ligand-binding domain; unp residues 402-539; unp residues 661-802	Mutation：S758T Mutation：S758T	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；300 K；PEG2000MME and HEPES, pH 7, VAPOR DIFFUSION, temperature 300K	Resolution 1.86 Å R-free 0.218
5DEX Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, phenyl-ACEPC Deposited 2015-08-26	Different construct 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 402–539（138 aa） Fragment：UNP residues 402-539, 661-802 Chain B 661–802（142 aa） Fragment：UNP residues 402-539, 661-802	Not recorded	GLY GLYCINE × 1 5E0 5-[(2R)-2-amino-2-carboxyethyl]-1-phenyl-1H-pyrazole-3-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；AMMONIUM ACETATE, PEG 4000	Resolution 2.40 Å R-free 0.285
5I56 Agonist-bound GluN1/GluN2A agonist binding domains with TCN201 Deposited 2016-02-14	Different construct 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 402–539（138 aa） Chain B 661–800（140 aa）	Not recorded	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 67P N-({4-[2-(benzenecarbonyl)hydrazinecarbonyl]phenyl}methyl)-3-chloro-4-fluorobenzene-1-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M ammonium sulfate and 16-22% PEG 4000	Resolution 2.28 Å R-free 0.239
5I57 Glutamate- and glycine-bound GluN1/GluN2A agonist binding domains Deposited 2016-02-14	Different construct 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 402–539（138 aa） Fragment：unp residues 402-539; 661-800 Chain B 661–800（140 aa） Fragment：unp residues 402-539; 661-800	Not recorded	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M ammonium sulfate and 16-22% PEG 4000	Resolution 1.70 Å R-free 0.222
5I58 GLUTAMATE- AND GLYCINE-BOUND GLUN1/GLUN2A AGONIST BINDING DOMAINS WITH MPX-004 Deposited 2016-02-14	Different construct 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 402–539（138 aa） Chain B 661–800（140 aa）	Not recorded	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 67R 5-({[(3-chloro-4-fluorophenyl)sulfonyl]amino}methyl)-N-[(2-methyl-1,3-thiazol-5-yl)methyl]pyrazine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；273 K；0.2 M ammonium sulfate and 16-22% PEG 4000	Resolution 2.52 Å R-free 0.292
5I59 Glutamate- and glycine-bound GluN1/GluN2A agonist binding domains with MPX 007 Deposited 2016-02-14	Different construct 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 402–539（138 aa） Chain B 661–800（140 aa）	Not recorded	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 67Q 5-({[(3,4-difluorophenyl)sulfonyl]amino}methyl)-6-methyl-N-[(2-methyl-4H-1lambda~4~,3-thiazol-5-yl)methyl]pyrazine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M ammonium sulfate and 16-22% PEG 4000	Resolution 2.25 Å R-free 0.264
5JTY Glutamate- and DCKA-bound GluN1/GluN2A agonist binding domains with MPX-007 Deposited 2016-05-10	Different construct 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 402–539（138 aa） Fragment：unp residues 402-539; 661-800 Chain B 661–800（140 aa） Fragment：unp residues 402-539; 661-800	Not recorded	2JK 4-hydroxy-5,7-dimethylquinoline-2-carboxylic acid × 1 6ND 5-({[(3,4-difluorophenyl)sulfonyl]amino}methyl)-6-methyl-N-[(2-methyl-1,3-thiazol-5-yl)methyl]pyrazine-2-carboxamide × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M AMMONIUM SULFATE AND 16-22% PEG 4000	Resolution 2.72 Å R-free 0.278
5TPW Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in complex with zinc at the GluN2A Deposited 2016-10-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 34–393（360 aa） Fragment：residues 34-393	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 6 GOL GLYCEROL × 2 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；1.8M Ammonium sulfate 2.5% Isopropanol	Resolution 2.91 Å R-free 0.245
5TQ0 Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in the presence of EDTA Deposited 2016-10-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 34–393（360 aa） Fragment：residues 34-393	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 2 SO4 SULFATE ION × 12 IPA ISOPROPYL ALCOHOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；1.8 M Ammonium sulfate, 2.5% Isopropanol	Resolution 2.70 Å R-free 0.246
5TQ2 Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in complex with zinc at GluN1 and GluN2A Deposited 2016-10-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 34–393（360 aa） Fragment：residues 34-393	Not recorded	ZN ZINC ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；1.8M Ammonium sulfate, 2.5% Isopropanol	Resolution 3.29 Å R-free 0.261
5VIH Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-fluorophenyl-ACEPC Deposited 2017-04-16	Different construct 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 402–539（138 aa） Chain B 661–802（142 aa）	Not recorded	GLY GLYCINE × 1 5DZ 5-[(2R)-2-amino-2-carboxyethyl]-1-(4-fluorophenyl)-1H-pyrazole-3-carboxylic acid × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonia Acetate, PEG 4000	Resolution 2.40 Å R-free 0.272
5VII Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-(3-fluoropropyl)phenyl-ACEPC Deposited 2017-04-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 402–539（138 aa）	Not recorded	GLY GLYCINE × 1 5DY 5-[(2R)-2-amino-2-carboxyethyl]-1-[4-(3-fluoropropyl)phenyl]-1H-pyrazole-3-carboxylic acid × 1 PEG DI(HYDROXYETHYL)ETHER × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonia Acetate, PEG 4000	Resolution 1.95 Å R-free 0.259
5VIJ Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-bromophenyl-ACEPC Deposited 2017-04-16	Different construct 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 402–539（138 aa） Chain B 661–802（142 aa）	Not recorded	GLY GLYCINE × 1 5DX 5-[(2R)-2-amino-2-carboxyethyl]-1-(4-bromophenyl)-1H-pyrazole-3-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonia Acetate, PEG 4000	Resolution 2.10 Å R-free 0.255
6MM9 Diheteromeric NMDA receptor GluN1/GluN2A in the '1-Knuckle' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 6.1 Deposited 2018-09-29	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34	ELECTRON MICROSCOPY cryo-EM buffer pH 6.1 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 5.97 Å
6MMA Diheteromeric NMDA receptor GluN1/GluN2A in the 'Extended' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 6.1 Deposited 2018-09-29	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34	ELECTRON MICROSCOPY cryo-EM buffer pH 6.1 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 6.31 Å
6MMB Diheteromeric NMDA receptor GluN1/GluN2A in the 'Super-Splayed' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 6.1 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34	ELECTRON MICROSCOPY cryo-EM buffer pH 6.1 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 12.70 Å
6MMG Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar EDTA, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 6.23 Å
6MMH Diheteromeric NMDA receptor GluN1/GluN2A in the 'Extended-2' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar zinc chloride, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 8.21 Å
6MMI Diheteromeric NMDA receptor GluN1/GluN2A in the 'Splayed-Open' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar zinc chloride, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 8.93 Å
6MMJ Diheteromeric NMDA receptor GluN1/GluN2A in the 'Super-Splayed' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar zinc chloride, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 16.50 Å
6MMK Diheteromeric NMDA receptor GluN1/GluN2A in the '1-Knuckle' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 6.08 Å
6MML Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Asymmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 7.14 Å
6MMM Diheteromeric NMDA receptor GluN1/GluN2A in the 'Extended-1' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-09-30	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 6.84 Å
6MMN Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 8.0 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 22	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 7.51 Å
6MMP Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 0.1 millimolar EDTA, and at pH 8.0 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；sample was blotted for 3 seconds at blot force 1.	Resolution 6.88 Å
6MMR Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar zinc chloride, 3 millimolar EDTA, and at pH 7.4 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 5.13 Å
6MMS Triheteromeric NMDA receptor GluN1/GluN2A/GluN2A* in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar EDTA, and at pH 7.4 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Mutation：H128S, N687Q Mutation：H128S, N687Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 29	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 5.38 Å
6MMT Triheteromeric NMDA receptor GluN1/GluN2A/GluN2A* in the '1-Knuckle' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Mutation：H128S, N687Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 29	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 7.46 Å
6MMU Triheteromeric NMDA receptor GluN1/GluN2A/GluN2A* in the '2-Knuckle-Asymmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Mutation：H128S, N687Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 5.30 Å
6MMV Triheteromeric NMDA receptor GluN1/GluN2A/GluN2A* Extracellular Domain in the '2-Knuckle-Asymmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-10-01	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 1–800（800 aa） Fragment：UNP residues 1-800 Chain D 1–800（800 aa） Fragment：UNP residues 1-800	Mutation：H128S, N687Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 4.71 Å
6MMW Triheteromeric NMDA receptor GluN1/GluN2A/GluN2A* in the '2-Knuckle-Symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Mutation：H128S, N687Q Mutation：H128S, N687Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 6.20 Å
6MMX Triheteromeric NMDA receptor GluN1/GluN2A/GluN2A* in the 'Extended' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at pH 7.4 Deposited 2018-10-01	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 1–837（837 aa） Fragment：UNP residues 1-837 Chain D 1–837（837 aa） Fragment：UNP residues 1-837	Mutation：H128S, N687Q Mutation：H128S, N687Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 25	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Sample was blotted for 3 seconds at blot force 1.	Resolution 6.99 Å
6ODL Crystal structure of GluN2A agonist binding domain with 4-butyl-(S)-CCG-IV Deposited 2019-03-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 404–539（136 aa） Chain B 404–539（136 aa）	Not recorded	M7V (1S,2R)-2-[(S)-amino(carboxy)methyl]-1-butylcyclopropane-1-carboxylic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M AMMONIUM SULFATE AND 16-22% PEG 4000	Resolution 2.30 Å R-free 0.283
6OVD Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 3-ethylphenyl-ACEPC Deposited 2019-05-07	Different construct 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 402–539（138 aa） Chain B 661–802（142 aa）	Not recorded	GLY GLYCINE × 1 N9A (3S,5S)-5-[(2R)-2-amino-2-carboxyethyl]-1-(3-ethylphenyl)pyrazolidine-3-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M AMMONIUM SULFATE AND 16-22% PEG 4000	Resolution 2.10 Å R-free 0.240
6OVE Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-propylphenyl-ACEPC Deposited 2019-05-07	Different construct 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 402–539（138 aa） Chain B 662–801（140 aa）	Not recorded	GLY GLYCINE × 1 N9D (3R,5S)-5-[(2R)-2-amino-2-carboxyethyl]-1-(4-propylphenyl)pyrazolidine-3-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M AMMONIUM SULFATE AND 16-22% PEG 4000	Resolution 2.00 Å R-free 0.216
6OVE Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-propylphenyl-ACEPC Deposited 2019-05-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 402–539（138 aa） Chain B 662–801（140 aa）	Not recorded	N9D (3R,5S)-5-[(2R)-2-amino-2-carboxyethyl]-1-(4-propylphenyl)pyrazolidine-3-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M AMMONIUM SULFATE AND 16-22% PEG 4000	Resolution 2.00 Å R-free 0.216
6USU Crystal structure of GluN1/GluN2A ligand-binding domain in complex with L689,560 and glutamate Deposited 2019-10-28	Different construct 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 402–539（138 aa） Fragment：UNP residues 402-539, 661-802 Chain B 661–802（142 aa） Fragment：UNP residues 402-539, 661-802	Not recorded	QGM (2R,4S)-5,7-dichloro-4-[(phenylcarbamoyl)amino]-1,2,3,4-tetrahydroquinoline-2-carboxylic acid × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；291 K；0.2 M HEPES, pH 7.0, 60-90 mM sodium chloride, 15-20% PEG2000 MME	Resolution 2.09 Å R-free 0.222
6USV Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and SDZ 220-040 Deposited 2019-10-28	Different construct 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 402–539（138 aa） Fragment：UNP residues 402-539, 661-802 Chain B 661–802（142 aa） Fragment：UNP residues 402-539, 661-802	Not recorded	GLY GLYCINE × 1 QGP (2S)-2-amino-3-[2',4'-dichloro-4-hydroxy-5-(phosphonomethyl)biphenyl-3-yl]propanoic acid × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；291 K；0.2 M HEPES, pH 7.0, 60-90 mM sodium chloride, 15-20% PEG2000 MME	Resolution 2.30 Å R-free 0.259
6UZ6 Crystal structure of GLUN1/GLUN2A-4M mutant ligand-binding domain in complex with glycine and glutamate Deposited 2019-11-14	Different construct 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 402–539（138 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-800) Chain B 661–800（140 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-800)	Mutation：A414R, K738M, G740R, R741K Mutation：A414R, K738M, G740R, R741K	GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；100 mM HEPES, pH 7.0, 75 mM sodium chloride, 18% PEG2000 MME	Resolution 1.66 Å R-free 0.212
6UZG Crystal structure of GLUN1/GLUN2A-4M mutant ligand-binding domain in complex with glycine and homoquinolinic acid Deposited 2019-11-15	Different construct 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 402–539（138 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802) Chain B 661–802（142 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802)	Mutation：A414R, K738M, G740R, R741K Mutation：A414R, K738M, G740R, R741K	GLY GLYCINE × 1 QM1 3-(carboxymethyl)pyridine-2-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；100 mM HEPES, pH 7.0, 75 mM sodium chloride, 18% PEG2000 MME	Resolution 1.94 Å R-free 0.250
6UZR Crystal structure of GLUN1/GLUN2A ligand-binding domain in complex with glycine and homoquinolinic acid Deposited 2019-11-15	Different construct 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 402–539（138 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802) Chain B 661–802（142 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802)	Not recorded	GLY GLYCINE × 1 GOL GLYCEROL × 3 QM1 3-(carboxymethyl)pyridine-2-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；100 mM HEPES, pH 7.0, 75 mM sodium chloride, 18% PEG2000 MME	Resolution 1.87 Å R-free 0.207
6UZW Crystal structure of GLUN1/GLUN2A ligand-binding domain in complex with glycine and UBP791 Deposited 2019-11-15	Different construct 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 402–539（138 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802) Chain B 661–802（142 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802)	Not recorded	GLY GLYCINE × 1 QM4 (2S,3R)-1-[7-(2-carboxyethyl)phenanthrene-2-carbonyl]piperazine-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；100 mM HEPES, pH 7.0, 75 mM sodium chloride, 18% PEG2000 MME	Resolution 2.13 Å R-free 0.247
6UZX Crystal structure of GLUN1/GLUN2A-4M mutant ligand-binding domain in complex with glycine and UBP791 Deposited 2019-11-15	Different construct 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 402–539（138 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802) Chain B 661–802（142 aa） Fragment：ligand-binding domain (UNP residues 402-539,661-802)	Mutation：A414R, K738M, G740R, R741K Mutation：A414R, K738M, G740R, R741K	GOL GLYCEROL × 2 GLY GLYCINE × 1 QM4 (2S,3R)-1-[7-(2-carboxyethyl)phenanthrene-2-carbonyl]piperazine-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；100 mM HEPES, pH 7.0, 75 mM sodium chloride, 18% PEG2000 MME	Resolution 2.41 Å R-free 0.245
8JF7 Triheteromeric NMDA receptor GluN1-GluN2A-GluN3A in complex with glycine, glutamate, a GluN1-specific Fab,and a GluN2A-specific Fab Deposited 2023-05-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 10 PDB declaration: decameric	Chain B 1–842（842 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.73 Å
8XLK Structure of native tri-heteromeric GluN1-GluN2A-GluN2B NMDA receptor in rat cortex and hippocampus Deposited 2023-12-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain B 1–1464（1464 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 7RC (2R)-4-(3-phosphonopropyl)piperazine-2-carboxylic acid × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
9C7C Diheteromeric GluN1/GluN2A (delM653) in nanodisc complexed with glycine, glutamate, and GNE-4123, open conformation Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–865（865 aa） Chain D 1–865（865 aa）	Not recorded	A1AUV 4-cyclohexyl-N-[(8R)-2-cyclopropyl-7-hydroxy-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-6-yl]benzene-1-sulfonamide × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 HP6 HEPTANE × 1 Y01 CHOLESTEROL HEMISUCCINATE × 8 GLY GLYCINE × 2 D12 DODECANE × 2 GLU GLUTAMIC ACID × 2 D10 DECANE × 2 HEX HEXANE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9C7E Diheteromeric GluN1/GluN2A (delM653) in nanodisc complex with glycine, glutamate, and GNE-4123, open conformation, C2 symmetry Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	A1AUV 4-cyclohexyl-N-[(8R)-2-cyclopropyl-7-hydroxy-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-6-yl]benzene-1-sulfonamide × 2 Y01 CHOLESTEROL HEMISUCCINATE × 6 D12 DODECANE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.22 Å
9C7P Diheteromeric GluN1/GluN2A (delM653) in digitonin complexed with glycine, glutamate, and GNE-4123 Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.61 Å
9C7Q Diheteromeric NMDA receptor GluN1/GluN2A, in complex with glycine and glutamate Deposited 2024-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.05 Å
9C7R Diheteromeric GluN1/GluN2A (M817V) in digitonin complexed with glycine, glutamate, and GNE-4123 Deposited 2024-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.99 Å
9NYZ Crystal structure of DCKA/glutamate-bound GluN1/GluN2A agonist binding domains with UCM-101 Deposited 2025-03-30	Different construct 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 402–539（138 aa） Chain B 661–802（142 aa）	Not recorded	DK1 5,7-DICHLORO-4-HYDROXYQUINOLINE-2-CARBOXYLIC ACID × 1 A1B7E N-(cyclohexylmethyl)-2-[(5-{[(1R)-1-phenylpropyl]amino}-1,3,4-thiadiazol-2-yl)sulfanyl]acetamide × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；ammonium acetate, PEG 4000	Resolution 1.71 Å R-free 0.202
9PZQ GluN1/GluN2A in complex with polyclonal autoantibody Fab fragments (class 1), glycine- and glutamate-bound state Deposited 2025-08-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.07 Å
9PZR GluN1/GluN2A in complex with polyclonal autoantibody Fab fragments (class 2), glycine- and glutamate-bound state Deposited 2025-08-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.92 Å
9PZW GluN1/GluN2A in complex with 3D2 Fab, glycine and glutamate-bound state Deposited 2025-08-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–866（866 aa） Chain D 1–866（866 aa）	Not recorded	GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 GLU GLUTAMIC ACID × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
9PZX GluN1/GluN2A in complex with 3D2 Fab, local ATD dimer Deposited 2025-08-11	Different construct 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 1–866（866 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.76 Å

59 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NMDE1_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–283； UniProt 402–802

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	9da9
Deposition date deposition_date	2024-08-22
Structure title title	Crystal structure of GluN1/GluN2A agonist-binding domains in complex with 7CKA and glutamate
Keywords keywords	Glutamate receptor Ligand-gated ion channel Neurotransmitter receptor Synaptic transmission Neuropharmacology, SIGNALING PROTEIN; SIGNALING PROTEIN
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	25.94 Å
Radius of gyration Rg (electron density) rg_electron	24.67 Å
Forward intensity I(0) i0	66821900.00
Molecular weight molecular_weight	63832.0 kDa
Excluded volume excluded_volume	79959 Å³
Envelope volume envelope_volume	97434 Å³
Hydration-shell volume shell_volume	32227 Å³
Envelope diameter envelope_diameter	90.7 Å
Shell Rg shell_rg	32.55 Å
Envelope Rg envelope_rg	25.04 Å
Shape Rg shape_rg	24.65 Å
Total Rg total_rg	25.61 Å
Total atoms total_atoms	8926
Residues n_residues	560
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	86.2 Å
Rg (real space) rg_real	25.83 Å
Rg uncertainty (real space) rg_real_error	0.59 Å
I(0) (real space) i0_real	6.6820e+07
I(0) uncertainty (real space) i0_real_error	9.1590e+05
Rg (reciprocal space) rg_reciprocal	25.86 Å
I(0) (reciprocal space) i0_reciprocal	66820000.0000
Solution quality estimate total_estimate	0.8772
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	32.5 Å
Skewness Skewness skewness	0.231
Kurtosis Kurtosis kurtosis	-0.276
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12550000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.953

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Glutamate receptor ionotropic, NMDA 1
Molecular weight formula_weight	33340.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	9318

GMSTRLKIVTIHQEPFVYVKPTMSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKGTRITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDS

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Glutamate receptor ionotropic, NMDA 2A
Molecular weight formula_weight	31785.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRGTQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTRFNQRGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHN

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	7-Chlorokynurenic acid
Molecular weight formula_weight	223.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLUTAMIC ACID
Molecular weight formula_weight	147.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	202

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8. Citations (1)

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Unit-cell length a length_a	54.244 Å
Unit-cell length b length_b	87.338 Å
Unit-cell length c length_c	135.896 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	4

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

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	33.970 Å
R factor r_factor	0.1709
R_work r_work	0.1679
R_free r_free	0.2281

fit	/app/data/saxs_computation/da/9da9/9da9.fit
pddf	/app/data/pr_computation/da/9da9/9da9.pr.out
profile	/app/data/saxs_computation/da/9da9/9da9.dat

Crystal structure of GluN1/GluN2A agonist-binding domains in complex with 7CKA and glutamate

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

Glutamate receptor ionotropic, NMDA 1

State in the Current Structure

Other States of the Same Protein in the Database

Glutamate receptor ionotropic, NMDA 2A

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)