9t9p

Adenosine receptor A2a (A2AR)-beta-lactamase fusion bound to beta-lactamase inhibitory protein II (BLIPII) and ZM241385

Method: ELECTRON MICROSCOPY Dmax: 131.6 Å Quality: REASONABLE

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

Beta-lactamase inhibitory protein II

Streptomyces exfoliatus

UniProt O87916

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 41–311 Not recorded Adenosine receptor A2a,Small exopenicillinase,Green fluorescent protein × 1 (P29274,P00808,P42212) ZMA 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

3 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O87916_STREX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–272; UniProt 41–311

Adenosine receptor A2a,Small exopenicillinase,Green fluorescent protein

Aequorea victoria

UniProt P00808

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 B; UniProt 47–300 Not recorded Beta-lactamase inhibitory protein II × 1 (O87916) ZMA 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

25 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLAC_BACLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 239–492; UniProt 47–300

Adenosine receptor A2a,Small exopenicillinase,Green fluorescent protein

Aequorea victoria

UniProt P29274

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 B; UniProt 2–214 Chain B; UniProt 220–316 Not recorded Beta-lactamase inhibitory protein II × 1 (O87916) ZMA 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

185 other PDB entries and 189 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AA2AR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 25–237; UniProt 2–214 Author chain B; PDBConstruct 495–591; UniProt 220–316

Adenosine receptor A2a,Small exopenicillinase,Green fluorescent protein

Aequorea victoria

UniProt P42212

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 B; UniProt 2–238 Not recorded Beta-lactamase inhibitory protein II × 1 (O87916) ZMA 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 600–836; UniProt 2–238

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 9t9p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t9p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t9p
Deposition date deposition_date2025-11-24
Structure title titleAdenosine receptor A2a (A2AR)-beta-lactamase fusion bound to beta-lactamase inhibitory protein II (BLIPII) and ZM241385
Keywords keywordsG-protein coupled receptor, GPCR, fusion tag, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.00
Radius of gyration Rg (electron density) rg_electron40.24
Forward intensity I(0) i0109530000.00
Molecular weight molecular_weight86703.0 kDa
Excluded volume excluded_volume109550 ų
Envelope volume envelope_volume149490 ų
Hydration-shell volume shell_volume34971 ų
Envelope diameter envelope_diameter142.9
Shell Rg shell_rg40.18
Envelope Rg envelope_rg39.70
Shape Rg shape_rg40.20
Total Rg total_rg40.36
Total atoms total_atoms6115
Residues n_residues803
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 dmax131.6
Rg (real space) rg_real39.87
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real1.0950e+08
I(0) uncertainty (real space) i0_real_error2.1280e+06
Rg (reciprocal space) rg_reciprocal39.34
I(0) (reciprocal space) i0_reciprocal109500000.0000
Solution quality estimate total_estimate0.6384
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.643
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24660000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.296; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.418; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)