6ffi

Crystal Structure of mGluR5 in complex with MMPEP at 2.2 A

Method: X-RAY DIFFRACTION Dmax: 92.8 Å Quality: REASONABLE

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

Metabotropic glutamate receptor 5,Endolysin,Metabotropic glutamate receptor 5

Homo sapiens

UniProt P00720

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–162 Fragment:MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5 Mutation:;E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A ; Non-standard monomer:Yes (specific site not provided by mmCIF) OLA OLEIC ACID × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 D8B 2-[2-(3-methoxyphenyl)ethynyl]-6-methyl-pyridine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.8;293.1 K;24-34% V/V PEG400, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8 Resolution 2.20 Å R-free 0.269

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.

721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENLYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 114–274; UniProt 2–162

Metabotropic glutamate receptor 5,Endolysin,Metabotropic glutamate receptor 5

Homo sapiens

UniProt P41594

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 569–678 Chain A; UniProt 680–836 Fragment:MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5,MGLUR5 Mutation:;E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A,E579A N667Y I669A G675M T742A S753A ; Non-standard monomer:Yes (specific site not provided by mmCIF) OLA OLEIC ACID × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 D8B 2-[2-(3-methoxyphenyl)ethynyl]-6-methyl-pyridine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.8;293.1 K;24-34% V/V PEG400, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8 Resolution 2.20 Å R-free 0.269

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.

28 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRM5_HUMAN
Isoform P41594-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–113; UniProt 569–678 Author chain A; PDBConstruct 275–431; UniProt 680–836

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

SAXS profile for 6ffi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ffi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ffi
Deposition date deposition_date2018-01-08
Structure title titleCrystal Structure of mGluR5 in complex with MMPEP at 2.2 A
Keywords keywords7TM, RECEPTOR, GPCR, MEMBRANE-PROTEIN, SIGNALING PROTEIN, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.33
Radius of gyration Rg (electron density) rg_electron27.86
Forward intensity I(0) i031307800.00
Molecular weight molecular_weight47602.0 kDa
Excluded volume excluded_volume61571 ų
Envelope volume envelope_volume77044 ų
Hydration-shell volume shell_volume24664 ų
Envelope diameter envelope_diameter94.7
Shell Rg shell_rg33.29
Envelope Rg envelope_rg27.76
Shape Rg shape_rg27.85
Total Rg total_rg28.55
Total atoms total_atoms3344
Residues n_residues409
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax92.8
Rg (real space) rg_real28.54
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real3.1310e+07
I(0) uncertainty (real space) i0_real_error4.5760e+05
Rg (reciprocal space) rg_reciprocal28.48
I(0) (reciprocal space) i0_reciprocal31310000.0000
Solution quality estimate total_estimate0.6633
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.8
Skewness Skewness skewness0.414
Kurtosis Kurtosis kurtosis-0.533
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6291000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 0.109; Positv: 1.000; Valcen: 0.782; Smooth: 0.857

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)