9lfa

Cryo-EM structure of human bradykinin receptor B1R bound to antagonist ELN441958

Method: ELECTRON MICROSCOPY Dmax: 98.5 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 256–279 Mutation:S124K/S132C Nanobody 6 × 1 A1EJF 7-chloranyl-2-[3-[(9-pyridin-4-yl-3,9-diazaspiro[5.5]undecan-3-yl)carbonyl]phenyl]-3H-isoindol-1-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–231 Chain A; UniProt 256–341 Mutation:S124K/S132C Nanobody 6 × 1 A1EJF 7-chloranyl-2-[3-[(9-pyridin-4-yl-3,9-diazaspiro[5.5]undecan-3-yl)carbonyl]phenyl]-3H-isoindol-1-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 9lfa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9lfa
Deposition date deposition_date2025-01-08
Structure title titleCryo-EM structure of human bradykinin receptor B1R bound to antagonist ELN441958
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_guinier27.57
Radius of gyration Rg (electron density) rg_electron27.40
Forward intensity I(0) i052018500.00
Molecular weight molecular_weight39615.0 kDa
Excluded volume excluded_volume39353 ų
Envelope volume envelope_volume67347 ų
Hydration-shell volume shell_volume22641 ų
Envelope diameter envelope_diameter103.8
Shell Rg shell_rg31.63
Envelope Rg envelope_rg27.92
Shape Rg shape_rg27.34
Total Rg total_rg27.86
Total atoms total_atoms3032
Residues n_residues390
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 dmax98.5
Rg (real space) rg_real27.99
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real5.2020e+07
I(0) uncertainty (real space) i0_real_error8.4700e+05
Rg (reciprocal space) rg_reciprocal27.86
I(0) (reciprocal space) i0_reciprocal52010000.0000
Solution quality estimate total_estimate0.7884
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.616
Kurtosis Kurtosis kurtosis-0.215
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7309000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.591; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.536; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)