8wst

Cryo-EM structure of Melanin-Concentrating Hormone Receptor 2 with MCH

Method: ELECTRON MICROSCOPY Dmax: 119.0 Å Quality: GOOD

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

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 2–340 Not recorded Guanine nucleotide-binding protein G(q) subunit alpha-1 × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Pro-MCH × 1 (P20382) NB35 × 1 Melanin-concentrating hormone receptor 2 × 1 (Q969V1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.04 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 9–347; UniProt 2–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Homo sapiens

UniProt P59768

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–71 Not recorded Guanine nucleotide-binding protein G(q) subunit alpha-1 × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Pro-MCH × 1 (P20382) NB35 × 1 Melanin-concentrating hormone receptor 2 × 1 (Q969V1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.04 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

1233 other PDB entries and 1236 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

Pro-MCH

Homo sapiens

UniProt P20382

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 147–165 Not recorded Guanine nucleotide-binding protein G(q) subunit alpha-1 × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) NB35 × 1 Melanin-concentrating hormone receptor 2 × 1 (Q969V1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.04 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCH_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain L; PDBConstruct 1–19; UniProt 147–165

Melanin-concentrating hormone receptor 2

Homo sapiens

UniProt Q969V1

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 1–331 Mutation:L256Y Guanine nucleotide-binding protein G(q) subunit alpha-1 × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Pro-MCH × 1 (P20382) NB35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.04 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MCHR2_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain R; PDBConstruct 1–331; UniProt 1–331

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 8wst

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wst
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wst
Deposition date deposition_date2023-10-17
Structure title titleCryo-EM structure of Melanin-Concentrating Hormone Receptor 2 with MCH
Keywords keywordsMelanin-Concentrating Hormone Receptors2, GPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.00
Radius of gyration Rg (electron density) rg_electron35.12
Forward intensity I(0) i0214148000.00
Molecular weight molecular_weight117990.0 kDa
Excluded volume excluded_volume147800 ų
Envelope volume envelope_volume191870 ų
Hydration-shell volume shell_volume46539 ų
Envelope diameter envelope_diameter129.5
Shell Rg shell_rg40.55
Envelope Rg envelope_rg35.24
Shape Rg shape_rg35.11
Total Rg total_rg35.53
Total atoms total_atoms8286
Residues n_residues1055
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 dmax119.0
Rg (real space) rg_real35.12
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real2.1410e+08
I(0) uncertainty (real space) i0_real_error3.1900e+06
Rg (reciprocal space) rg_reciprocal35.05
I(0) (reciprocal space) i0_reciprocal214100000.0000
Solution quality estimate total_estimate0.8662
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary116.3
Skewness Skewness skewness0.473
Kurtosis Kurtosis kurtosis-0.176
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48670000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)