9lfc

Cryo-EM structure of human bradykinin receptor B1R bound to antagonist R715

Method: ELECTRON MICROSCOPY Dmax: 99.7 Å Quality: GOOD

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

B1 bradykinin receptor,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 Insufficient information Heteromer Protein × 3 PDB declaration: dimeric(2) Count mismatch; review required Chain A; UniProt 256–279 Mutation:S124K/S132C Nanobody 6 × 1 R715 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 1
Chains and sequence ranges Author chain A; PDBConstruct 231–254; UniProt 256–279

B1 bradykinin receptor,Kappa-type opioid receptor

Homo sapiens

UniProt P46663

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 Heteromer Protein × 3 PDB declaration: dimeric(2) Count mismatch; review required Chain A; UniProt 2–231 Chain A; UniProt 256–341 Mutation:S124K/S132C Nanobody 6 × 1 R715 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BKRB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–230; UniProt 2–231 Author chain A; PDBConstruct 255–340; UniProt 256–341

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 9lfc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9lfc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9lfc
Deposition date deposition_date2025-01-08
Structure title titleCryo-EM structure of human bradykinin receptor B1R bound to antagonist R715
Keywords keywordsGPCR, bradykinin receptor, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN-IMMUNE SYSTEM complex; MEMBRANE PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.30
Radius of gyration Rg (electron density) rg_electron27.46
Forward intensity I(0) i028315000.00
Molecular weight molecular_weight44119.0 kDa
Excluded volume excluded_volume56449 ų
Envelope volume envelope_volume70026 ų
Hydration-shell volume shell_volume23210 ų
Envelope diameter envelope_diameter105.2
Shell Rg shell_rg31.83
Envelope Rg envelope_rg28.21
Shape Rg shape_rg27.50
Total Rg total_rg27.84
Total atoms total_atoms3133
Residues n_residues406
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 dmax99.7
Rg (real space) rg_real28.71
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real2.8310e+07
I(0) uncertainty (real space) i0_real_error4.7040e+05
Rg (reciprocal space) rg_reciprocal28.59
I(0) (reciprocal space) i0_reciprocal28310000.0000
Solution quality estimate total_estimate0.7913
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6473000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.632; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.456; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)