SAXSdb — 7wih

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

Metabotropic glutamate receptor 3

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 23–879 Chain B； UniProt 23–879	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CWY (1S,2S,4S,5R,6S)-2-amino-4-[(3-methoxybenzene-1-carbonyl)amino]bicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.68 Å

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 7WIH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3SM9 Crystal Structure of Metabotropic glutamate receptor 3 precursor in presence of LY341495 antagonist Deposited 2011-06-27	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 26–504（479 aa）	Not recorded	SO4 SULFATE ION × 10 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.5 M Ammonium Sulfate 0.1 M BisTris Propane pH 7.0 , VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.26 Å R-free 0.227
4XAR mGluR2 ECD and mGluR3 ECD complex with ligands Deposited 2014-12-15	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–508（507 aa） Fragment：UNP RESIDUES 2-508	Not recorded	40F (1S,2S,5R,6S)-2-aminobicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 2 IOD IODIDE ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；20% PEG 3350, 200mM Ammonium Iodide	Resolution 2.26 Å R-free 0.224
5CNK mglur3 with glutamate Deposited 2015-07-17	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	GLU GLUTAMIC ACID × 2 IOD IODIDE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；16% PEG 3350 + 200mM Ammonium Iodide, 50mM Tris pH 8.0 / 150mM NaCl	Resolution 3.15 Å R-free 0.258
5CNK mglur3 with glutamate Deposited 2015-07-17	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 2–507（506 aa） Fragment：UNP residues 2-507 Chain C 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	IOD IODIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；16% PEG 3350 + 200mM Ammonium Iodide, 50mM Tris pH 8.0 / 150mM NaCl	Resolution 3.15 Å R-free 0.258
5CNK mglur3 with glutamate Deposited 2015-07-17	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 2–507（506 aa） Fragment：UNP residues 2-507 Chain C 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	IOD IODIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；16% PEG 3350 + 200mM Ammonium Iodide, 50mM Tris pH 8.0 / 150mM NaCl	Resolution 3.15 Å R-free 0.258
5CNK mglur3 with glutamate Deposited 2015-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	GLU GLUTAMIC ACID × 1 IOD IODIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；16% PEG 3350 + 200mM Ammonium Iodide, 50mM Tris pH 8.0 / 150mM NaCl	Resolution 3.15 Å R-free 0.258
5CNK mglur3 with glutamate Deposited 2015-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	IOD IODIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；16% PEG 3350 + 200mM Ammonium Iodide, 50mM Tris pH 8.0 / 150mM NaCl	Resolution 3.15 Å R-free 0.258
5CNK mglur3 with glutamate Deposited 2015-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	IOD IODIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；16% PEG 3350 + 200mM Ammonium Iodide, 50mM Tris pH 8.0 / 150mM NaCl	Resolution 3.15 Å R-free 0.258
5CNM mGluR3 complexed with glutamate analog Deposited 2015-07-17	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	52Q (1R,2S,4R,5R,6R)-2-amino-4-(1H-1,2,4-triazol-3-ylsulfanyl)bicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 2 CL CHLORIDE ION × 4 SO4 SULFATE ION × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；100mM Hepes pH 7.7 + 19% PEG 8K + 50mM Magnesium Sulfate	Resolution 2.84 Å R-free 0.226
5CNM mGluR3 complexed with glutamate analog Deposited 2015-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–507（506 aa） Fragment：UNP residues 2-507	Not recorded	52Q (1R,2S,4R,5R,6R)-2-amino-4-(1H-1,2,4-triazol-3-ylsulfanyl)bicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 1 CL CHLORIDE ION × 2 SO4 SULFATE ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；100mM Hepes pH 7.7 + 19% PEG 8K + 50mM Magnesium Sulfate	Resolution 2.84 Å R-free 0.226
6B7H Structure of mGluR3 with an agonist Deposited 2017-10-04	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 Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–507（506 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CWY (1S,2S,4S,5R,6S)-2-amino-4-[(3-methoxybenzene-1-carbonyl)amino]bicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；298 K；100 mM Bis-Tris, pH 5.5, 17% PEG10000, 100 mM ammonium acetate	Resolution 2.82 Å R-free 0.223
7WI6 Cryo-EM structure of LY341495/NAM-bound mGlu3 Deposited 2022-01-03	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 23–879（857 aa） Chain B 23–879（857 aa）	Not recorded	Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.71 Å
7WI8 Cryo-EM structure of inactive mGlu3 bound to LY341495 Deposited 2022-01-03	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 23–879（857 aa） Chain B 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.17 Å
8JCU Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 (dimerization mode I) Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8JCV Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 (dimerization mode II) Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8JCW Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 and NAM563 (dimerization mode I) Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8JCX Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 and NAM563 (dimerization mode II) Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8JCY Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and LY2389575 (dimerization mode I) Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2 CLR CHOLESTEROL × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8JCZ Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and LY2389575 (dimerization mode III) Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 Z99 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8JD0 Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of NAM563 Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 J9R 4-(1-methylpyrazol-4-yl)-7-[[(2~{S})-2-(trifluoromethyl)morpholin-4-yl]methyl]quinoline-2-carboxamide × 1 CLR CHOLESTEROL × 9 GLU GLUTAMIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8JD1 Cryo-EM structure of mGlu2-mGlu3 heterodimer in Rco state Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	GLU GLUTAMIC ACID × 2 CLR CHOLESTEROL × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8JD2 Cryo-EM structure of G protein-free mGlu2-mGlu3 heterodimer in Acc state Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain 3 23–879（857 aa）	Not recorded	GLU GLUTAMIC ACID × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8JD3 Cryo-EM structure of Gi1-bound mGlu2-mGlu3 heterodimer Deposited 2023-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain 3 23–879（857 aa）	Not recorded	HZR 1-butyl-3-chloranyl-4-(4-phenylpiperidin-1-yl)pyridin-2-one × 1 GLU GLUTAMIC ACID × 2 CLR CHOLESTEROL × 3 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9II2 Cryo-EM Structure of the 2:2 Complex of mGlu3 and beta-arrestin1 Deposited 2024-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–879（879 aa） Chain R 1–879（879 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GLU GLUTAMIC ACID × 2 CLR CHOLESTEROL × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
9II3 Cryo-EM Structure of the 2:1 Complex of mGlu3 and beta-arrestin1 Deposited 2024-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–879（879 aa） Chain R 1–879（879 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GLU GLUTAMIC ACID × 2 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

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

View Construct and Data Evidence

UniProt name	GRM3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 31–887； UniProt 23–879 Author chain B； PDBConstruct 31–887； UniProt 23–879

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	7wih
Deposition date deposition_date	2022-01-03
Structure title title	Cryo-EM structure of LY2794193-bound mGlu3
Keywords keywords	Glutamate, G protein-coupled receptor, Cryo-EM, Selective ligand, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	54.23 Å
Radius of gyration Rg (electron density) rg_electron	54.43 Å
Forward intensity I(0) i0	313963000.00
Molecular weight molecular_weight	141900.0 kDa
Excluded volume excluded_volume	175330 Å³
Envelope volume envelope_volume	286480 Å³
Hydration-shell volume shell_volume	48085 Å³
Envelope diameter envelope_diameter	178.2 Å
Shell Rg shell_rg	49.22 Å
Envelope Rg envelope_rg	54.83 Å
Shape Rg shape_rg	54.47 Å
Total Rg total_rg	54.10 Å
Total atoms total_atoms	10002
Residues n_residues	1482
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	169.4 Å
Rg (real space) rg_real	54.86 Å
Rg uncertainty (real space) rg_real_error	2.09 Å
I(0) (real space) i0_real	3.1400e+08
I(0) uncertainty (real space) i0_real_error	6.7530e+06
Rg (reciprocal space) rg_reciprocal	53.67 Å
I(0) (reciprocal space) i0_reciprocal	313400000.0000
Solution quality estimate total_estimate	0.7234
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	40.9 Å
Skewness Skewness skewness	0.469
Kurtosis Kurtosis kurtosis	-0.845
Angular range angular_range	— – 0.1450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	16070000.0000
Real-space data points n_real_points	30
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.598; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.612; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Metabotropic glutamate receptor 3
Molecular weight formula_weight	100021.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	10002

MKTIIALSYIFCLVFADYKDDDDENLYFQGLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCTCMVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSSFAICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEAPGTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQKNVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSL

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	(1S,2S,4S,5R,6S)-2-amino-4-[(3-methoxybenzene-1-carbonyl)amino]bicyclo[3.1.0]hexane-2,6-dicarboxylic acid
Molecular weight formula_weight	334.3 kDa
Source method src_method	syn
Copy count entity_count	2

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	3.68 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	288762

fit	/app/data/saxs_computation/wi/7wih/7wih.fit
pddf	/app/data/pr_computation/wi/7wih/7wih.pr.out
profile	/app/data/saxs_computation/wi/7wih/7wih.dat

Cryo-EM structure of LY2794193-bound mGlu3

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

Metabotropic glutamate receptor 3

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

冷冻电镜 EM 3D