9xqb

Cryo-EM structure of the human A2A adenosine receptor in complex with a Fab antibody fragment

Method: ELECTRON MICROSCOPY Dmax: 100.2 Å Quality: GOOD

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

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息,但缺少统一蛋白身份时,不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly Oligomeric State 实体与Construct证据 Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer 蛋白 3 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: trimeric Entity 1:Fab Light chain × 1 Entity 2:A2A receptor-BRIL × 1 Entity 3:Fab Heavy chain × 1 缺少 UniProt 身份时不显示参考序列区间 Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 Å

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 9xqb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xqb
Deposition date deposition_date2025-11-18
Structure title titleCryo-EM structure of the human A2A adenosine receptor in complex with a Fab antibody fragment
Keywords keywordsCryo-EM Lip-MS, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.49
Radius of gyration Rg (electron density) rg_electron29.73
Forward intensity I(0) i031936900.00
Molecular weight molecular_weight41251.0 kDa
Excluded volume excluded_volume50456 ų
Envelope volume envelope_volume73748 ų
Hydration-shell volume shell_volume22917 ų
Envelope diameter envelope_diameter107.5
Shell Rg shell_rg32.91
Envelope Rg envelope_rg29.78
Shape Rg shape_rg29.66
Total Rg total_rg30.28
Total atoms total_atoms2932
Residues n_residues453
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 dmax100.2
Rg (real space) rg_real29.80
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real3.1940e+07
I(0) uncertainty (real space) i0_real_error5.3860e+05
Rg (reciprocal space) rg_reciprocal29.67
I(0) (reciprocal space) i0_reciprocal31930000.0000
Solution quality estimate total_estimate0.8129
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.541
Kurtosis Kurtosis kurtosis-0.426
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11500000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.662; Smooth: 0.827

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)