SAXSdb — 3fat

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

Glutamate receptor 4

Rattus norvegicus

UniProt P19493

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 415–528 Chain A； UniProt 654–796 Chain B； UniProt 415–528 Chain B； UniProt 654–796	Fragment：iGluR4 flip ligand-binding core (S1S2)	AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2 SO4 SULFATE ION × 5 GOL GLYCEROL × 5 ACY ACETIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG 4000, Acetate, (NH4)2SO4, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.90 Å R-free 0.216
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 415–528 Chain C； UniProt 654–796	Fragment：iGluR4 flip ligand-binding core (S1S2)	AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 8 ACY ACETIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG 4000, Acetate, (NH4)2SO4, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.90 Å R-free 0.216

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 3FAT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3EN3 Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate Deposited 2008-09-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 416–528（113 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958) Chain A 654–795（142 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958)	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；25.5% PEG 1500, 0.05M Na-Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.43 Å R-free 0.219
3EN3 Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate Deposited 2008-09-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 416–528（113 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958) Chain A 654–795（142 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958)	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；25.5% PEG 1500, 0.05M Na-Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.43 Å R-free 0.219
3EPE Crystal Structure of the GluR4 Ligand-Binding domain in complex with glutamate Deposited 2008-09-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 416–528（113 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958) Chain A 654–795（142 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958) Chain B 416–528（113 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958) Chain B 654–795（142 aa） Fragment：ligand binding domain (UNP residues 416-528 and 654-958)	Not recorded	GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；291 K；25% PEG 4000, 0.1M Na-Acetate pH 4.6, 0.2M Ammonium Sulphate, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.85 Å R-free 0.220
3FAS X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-glutamate at 1.40A resolution Deposited 2008-11-18	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 415–528（114 aa） Fragment：iGluR4 flip ligand-binding core (S1S2) Chain A 654–796（143 aa） Fragment：iGluR4 flip ligand-binding core (S1S2) Chain B 415–528（114 aa） Fragment：iGluR4 flip ligand-binding core (S1S2) Chain B 654–796（143 aa） Fragment：iGluR4 flip ligand-binding core (S1S2)	Not recorded	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 8 GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG4000, Acetate, (NH4)2SO4, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.40 Å R-free 0.183
3KEI Crystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with glutamate Deposited 2009-10-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 416–528（113 aa） Fragment：ligand binding domain Chain A 654–795（142 aa） Fragment：ligand binding domain Chain B 416–528（113 aa） Fragment：ligand binding domain Chain B 654–795（142 aa） Fragment：ligand binding domain	Mutation：L134V Mutation：L134V Mutation：L134V Mutation：L134V	GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；291 K；24% PEG 4000, 0.1M Na-Acetate, 0.3M Ammonium Sulphate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.90 Å R-free 0.224
3KFM Crystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with kainate Deposited 2009-10-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 416–528（113 aa） Fragment：ligand binding domain Chain A 654–795（142 aa） Fragment：ligand binding domain	Mutation：L134V Mutation：L134V	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；291 K；18% PEG 8000, 0.1M Na-Acetate, 0.2M Ammonium Sulphate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.20 Å R-free 0.274
4GPA High resolution structure of the GluA4 N-terminal domain (NTD) Deposited 2012-08-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–401（380 aa） Fragment：N-terminal domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.74M sodium citrate, 0.1M cacodylate pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291.0K	Resolution 2.25 Å R-free 0.235
5FWX Crystal structure of the AMPA receptor GluA2/A4 N-terminal domain heterodimer Deposited 2016-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 22–401（380 aa） Fragment：RESIDUES 22-401	Not recorded	SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions 17% PEG 3350 WITH 0.1-0.35 M AMMONIUM SULPHATE	Resolution 2.50 Å R-free 0.238
5FWX Crystal structure of the AMPA receptor GluA2/A4 N-terminal domain heterodimer Deposited 2016-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 22–401（380 aa） Fragment：RESIDUES 22-401	Not recorded	SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions 17% PEG 3350 WITH 0.1-0.35 M AMMONIUM SULPHATE	Resolution 2.50 Å R-free 0.238
9IGZ GluA4 in complex with TARP-2, resting state, structure of N-terminal domain Deposited 2025-02-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9NR6 The structure of Noelin 1 with cerebellar GluA1/A4-ATD Deposited 2025-03-14	Different construct 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 B 22–399（378 aa） Chain D 22–399（378 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
9NR7 The structure of GluA1/A4 LBD-TMD in Noelin-AMPAR complex Deposited 2025-03-14	Different construct 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 417–840（424 aa） Chain D 417–840（424 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.18 Å
9NR8 The structure of cerebellar GluA1/A4 ATD Deposited 2025-03-14	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 B 22–399（378 aa） Chain D 22–399（378 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 3.53 Å
9NR9 The structure of GluA1/A4 LBD-TMD with 2 TARPs Deposited 2025-03-14	Different construct 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 417–840（424 aa） Chain D 417–840（424 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.22 Å
9NRA The structure of GluA1/A4 LBD-TMD with 4 auxiliary subunits Deposited 2025-03-14	Different construct 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 417–840（424 aa） Chain D 417–840（424 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.18 Å
9P9B Activated GluA4 homotetrameric AMPAR. Deposited 2025-06-24	Different construct 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 A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
9P9C Active substate 1 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct 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 A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	CYZ CYCLOTHIAZIDE × 4 GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.01 Å
9P9D Active substate 2 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct 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 A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.82 Å
9P9E Active substate 3 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct 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 A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.82 Å
9P9F Active substate 4 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct 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 A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.89 Å
9P9G Active substate 5 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct 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 A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.06 Å
9QDN GluA4 in complex with TARP-2, resting state I, structure of TMD/LBD Deposited 2025-03-06	Different construct 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 A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	PLM PALMITIC ACID × 16 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.71 Å
9QPW GluA4, resting state, structure of TMD/LBD Deposited 2025-03-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9RMS GluA4 in complex with TARP-2, Resting II state, structure of TMD/LBD domains Deposited 2025-06-18	Different construct 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 A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9RMW GluA4 in complex with TARP-2, open state, structure of TMD/LBD domains Deposited 2025-06-18	Different construct 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 A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	PLM PALMITIC ACID × 18 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 CYZ CYCLOTHIAZIDE × 4 GLU GLUTAMIC ACID × 4 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9RN4 GluA4 in complex with TARP-2, desensitized state, structure of TMD/LBD domains Deposited 2025-06-19	Different construct 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 A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	PLM PALMITIC ACID × 4 CA CALCIUM ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9RN7 GluA4 in complex with TARP-2, Desensitized state, structure of TMD domain Deposited 2025-06-19	Different construct 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 A 21–902（882 aa） Chain B 21–902（882 aa） Chain C 21–902（882 aa） Chain D 21–902（882 aa）	Not recorded	PLM PALMITIC ACID × 4 CA CALCIUM ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

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

View Construct and Data Evidence

UniProt name	GRIA4_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–115； UniProt 415–528 Author chain A； PDBConstruct 118–260； UniProt 654–796 Author chain B； PDBConstruct 2–115； UniProt 415–528 Author chain B； PDBConstruct 118–260； UniProt 654–796 Author chain C； PDBConstruct 2–115； UniProt 415–528 Author chain C； PDBConstruct 118–260； UniProt 654–796

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3fat
Deposition date deposition_date	2008-11-18
Structure title title	X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-AMPA at 1.90A resolution
Keywords keywords	ionotropic glutamate receptors, iGluR4, flip, ligand-binding core, agonist complex, MEMBRANE PROTEIN; MEMBRANE 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	30.75 Å
Radius of gyration Rg (electron density) rg_electron	29.91 Å
Forward intensity I(0) i0	123008000.00
Molecular weight molecular_weight	89100.0 kDa
Excluded volume excluded_volume	112130 Å³
Envelope volume envelope_volume	138220 Å³
Hydration-shell volume shell_volume	38577 Å³
Envelope diameter envelope_diameter	106.8 Å
Shell Rg shell_rg	37.02 Å
Envelope Rg envelope_rg	30.03 Å
Shape Rg shape_rg	29.88 Å
Total Rg total_rg	30.67 Å
Total atoms total_atoms	6235
Residues n_residues	777
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	100.7 Å
Rg (real space) rg_real	30.71 Å
Rg uncertainty (real space) rg_real_error	0.62 Å
I(0) (real space) i0_real	1.2300e+08
I(0) uncertainty (real space) i0_real_error	1.8060e+06
Rg (reciprocal space) rg_reciprocal	30.73 Å
I(0) (reciprocal space) i0_reciprocal	123000000.0000
Solution quality estimate total_estimate	0.8929
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	36.8 Å
Skewness Skewness skewness	0.318
Kurtosis Kurtosis kurtosis	-0.347
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	40850000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.929

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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	Glutamate receptor 4
Molecular weight formula_weight	29020.5 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	6962

GRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECG

来源 Source

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

Entity 2 Entity 2 non-polymer

Description description	(S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID
Molecular weight formula_weight	186.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 5 Entity 5 non-polymer

Description description	ACETIC ACID
Molecular weight formula_weight	60.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	630

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d3fata1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

Domain ID domain_id	d3fata2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3fatb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

Domain ID domain_id	d3fatb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3fatc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

Domain ID domain_id	d3fatc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id	3fatA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3fatA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3fatB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3fatB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3fatC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	3fatC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

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8. Citations (1)

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Unit-cell length a length_a	105.175 Å
Unit-cell length b length_b	169.531 Å
Unit-cell length c length_c	73.883 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	120.58 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	32.644 Å
R factor r_factor	0.1770
R_work r_work	0.1750
R_free r_free	0.2160

fit	/app/data/saxs_computation/fa/3fat/3fat.fit
pddf	/app/data/pr_computation/fa/3fat/3fat.pr.out
profile	/app/data/saxs_computation/fa/3fat/3fat.dat

X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-AMPA at 1.90A resolution