SAXSdb — 6b7h

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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	Other combination Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2–507	Not recorded	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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 6B7H	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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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
7WI6 Cryo-EM structure of LY341495/NAM-bound mGlu3 Deposited 2022-01-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 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
7WIH Cryo-EM structure of LY2794193-bound mGlu3 Deposited 2022-01-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 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 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
8JCU Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 (dimerization mode I) Deposited 2023-05-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 method 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 method 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 4–509； UniProt 2–507

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	6b7h
Deposition date deposition_date	2017-10-04
Structure title title	Structure of mGluR3 with an agonist
Keywords keywords	mGluR3 Glutamate, MEMBRANE PROTEIN-AGONIST complex; MEMBRANE PROTEIN/AGONIST
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	23.82 Å
Radius of gyration Rg (electron density) rg_electron	22.81 Å
Forward intensity I(0) i0	42625900.00
Molecular weight molecular_weight	50397.0 kDa
Excluded volume excluded_volume	63047 Å³
Envelope volume envelope_volume	76070 Å³
Hydration-shell volume shell_volume	27383 Å³
Envelope diameter envelope_diameter	98.7 Å
Shell Rg shell_rg	30.08 Å
Envelope Rg envelope_rg	23.59 Å
Shape Rg shape_rg	22.76 Å
Total Rg total_rg	23.83 Å
Total atoms total_atoms	3553
Residues n_residues	441
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	95.6 Å
Rg (real space) rg_real	23.79 Å
Rg uncertainty (real space) rg_real_error	0.77 Å
I(0) (real space) i0_real	4.2630e+07
I(0) uncertainty (real space) i0_real_error	5.5520e+05
Rg (reciprocal space) rg_reciprocal	23.80 Å
I(0) (reciprocal space) i0_reciprocal	42630000.0000
Solution quality estimate total_estimate	0.7700
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.4 Å
Skewness Skewness skewness	0.411
Kurtosis Kurtosis kurtosis	-0.021
Angular range angular_range	— – 0.3350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	14930000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.415; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.763; Smooth: 0.997

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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	Metabotropic glutamate receptor 3
Molecular weight formula_weight	58776.6 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	3567

MALKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNISIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSEGHHHHHH

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	unidentified baculovirus

Entity 2 Entity 2 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 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	1

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	14

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d6b7ha1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.93 — Periplasmic binding protein-like I
Superfamily Superfamily superfamily	c.93.1 — Periplasmic binding protein-like I
Family Family family	c.93.1.0 — automated matches

Domain ID domain_id	d6b7ha2
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

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8. Citations (1)

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Unit-cell length a length_a	80.081 Å
Unit-cell length b length_b	80.081 Å
Unit-cell length c length_c	161.887 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.820 Å
Low-resolution limit resolution_low	25.280 Å
R factor r_factor	0.1852
R_work r_work	0.1840
R_free r_free	0.2231

fit	/app/data/saxs_computation/b7/6b7h/6b7h.fit
pddf	/app/data/pr_computation/b7/6b7h/6b7h.pr.out
profile	/app/data/saxs_computation/b7/6b7h/6b7h.dat

Structure of mGluR3 with an agonist

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

Refinement Refinement

Diffraction experiment Diffraction