22es

Gi bound kappa-opioid receptor in complex with difelikefalin

Method: ELECTRON MICROSCOPY Dmax: 125.7 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

Rattus norvegicus

UniProt P54311

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(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Kappa-type opioid receptor × 1 (P41145) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) scFv16 × 1 DPN-DPN-DLE-DLY-A1L9X × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.43 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.

161 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 16–354; UniProt 2–340

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

Bos taurus

UniProt P63212

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 C; UniProt 1–71 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) Kappa-type opioid receptor × 1 (P41145) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) scFv16 × 1 DPN-DPN-DLE-DLY-A1L9X × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.43 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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–71; UniProt 1–71

Kappa-type opioid receptor

Homo sapiens

UniProt P41145

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 3–380 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) scFv16 × 1 DPN-DPN-DLE-DLY-A1L9X × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.43 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.

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

View Construct and Data Evidence
UniProt name OPRK_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 12–389; UniProt 3–380

Guanine nucleotide-binding protein G(i) subunit alpha-1

Homo sapiens

UniProt P63096

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 D; UniProt 1–354 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Kappa-type opioid receptor × 1 (P41145) scFv16 × 1 DPN-DPN-DLE-DLY-A1L9X × 1 CLR CHOLESTEROL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.43 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.

573 other PDB entries and 591 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–354; UniProt 1–354

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 22es

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 22es
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id22es
Deposition date deposition_date2026-01-08
Structure title titleGi bound kappa-opioid receptor in complex with difelikefalin
Keywords keywordsGPCR, opioid receptor, SIGNALING PROTEIN/IMMUNE SYSTEM, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.98
Radius of gyration Rg (electron density) rg_electron37.85
Forward intensity I(0) i0479042000.00
Molecular weight molecular_weight119450.0 kDa
Excluded volume excluded_volume115970 ų
Envelope volume envelope_volume212830 ų
Hydration-shell volume shell_volume47896 ų
Envelope diameter envelope_diameter130.3
Shell Rg shell_rg42.41
Envelope Rg envelope_rg37.81
Shape Rg shape_rg37.86
Total Rg total_rg38.04
Total atoms total_atoms9028
Residues n_residues1137
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 dmax125.7
Rg (real space) rg_real37.93
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real4.7900e+08
I(0) uncertainty (real space) i0_real_error8.6030e+06
Rg (reciprocal space) rg_reciprocal37.97
I(0) (reciprocal space) i0_reciprocal479100000.0000
Solution quality estimate total_estimate0.8968
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.9
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44350000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)