8zwf

cryoEM structure of JR14a bound C3aR-BRIL-BAG2 complex

Method: ELECTRON MICROSCOPY Dmax: 137.3 Å Quality: REASONABLE

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

Beta-2 adrenergic receptor,C3a anaphylatoxin chemotactic receptor,Soluble cytochrome b562

Homo sapiens

UniProt P07550

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: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–30 Mutation:E27Q,M29W,H124I anti-BRIL Fab LC × 1 anti-BRIL Fab HC × 1 A1D9A (2~{S})-5-[bis(azanyl)methylideneamino]-2-[[5-[bis(4-chlorophenyl)methyl]-3-methyl-thiophen-2-yl]carbonylamino]pentanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

143 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADRB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–39; UniProt 1–30

Beta-2 adrenergic receptor,C3a anaphylatoxin chemotactic receptor,Soluble cytochrome b562

Homo sapiens

UniProt P0ABE7

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: trimeric(3) Consistent with protein copy count Chain A; UniProt 23–127 Mutation:E27Q,M29W,H124I anti-BRIL Fab LC × 1 anti-BRIL Fab HC × 1 A1D9A (2~{S})-5-[bis(azanyl)methylideneamino]-2-[[5-[bis(4-chlorophenyl)methyl]-3-methyl-thiophen-2-yl]carbonylamino]pentanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

714 other PDB entries and 822 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C562_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 416–520; UniProt 23–127

Beta-2 adrenergic receptor,C3a anaphylatoxin chemotactic receptor,Soluble cytochrome b562

Homo sapiens

UniProt Q16581

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: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–362 Chain A; UniProt 373–482 Mutation:E27Q,M29W,H124I anti-BRIL Fab LC × 1 anti-BRIL Fab HC × 1 A1D9A (2~{S})-5-[bis(azanyl)methylideneamino]-2-[[5-[bis(4-chlorophenyl)methyl]-3-methyl-thiophen-2-yl]carbonylamino]pentanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3AR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 49–410; UniProt 1–362 Author chain A; PDBConstruct 529–638; UniProt 373–482

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 8zwf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8zwf
Deposition date deposition_date2024-06-13
最后修订 last_revision2025-05-14
Structure title titlecryoEM structure of JR14a bound C3aR-BRIL-BAG2 complex
Keywords keywordscomplement receptor, C3aR, Non-peptide agonist, JR14a, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.91
Radius of gyration Rg (electron density) rg_electron40.51
Forward intensity I(0) i0225316000.00
Molecular weight molecular_weight81911.0 kDa
Excluded volume excluded_volume79678 ų
Envelope volume envelope_volume159650 ų
Hydration-shell volume shell_volume35691 ų
Envelope diameter envelope_diameter138.3
Shell Rg shell_rg41.47
Envelope Rg envelope_rg40.10
Shape Rg shape_rg40.49
Total Rg total_rg40.59
Total atoms total_atoms6207
Residues n_residues801
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 dmax137.3
Rg (real space) rg_real40.43
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real2.2530e+08
I(0) uncertainty (real space) i0_real_error4.3090e+06
Rg (reciprocal space) rg_reciprocal40.12
I(0) (reciprocal space) i0_reciprocal225200000.0000
Solution quality estimate total_estimate0.5828
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.455
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11410000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.726; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.538; Smooth: 0.671

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)