9ujm

Structure of a membrane protein

Method: ELECTRON MICROSCOPY Dmax: 65.0 Å Quality: REASONABLE

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

5-hydroxytryptamine receptor 2A

Homo sapiens

UniProt P28223

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 66–405 Not recorded A1L11 Pimavanserin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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.

38 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 5HT2A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 29–368; UniProt 66–405

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 9ujm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ujm
Deposition date deposition_date2025-04-17
Structure title titleStructure of a membrane protein
Keywords keywordsSerotonin Receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier19.92
Radius of gyration Rg (electron density) rg_electron18.68
Forward intensity I(0) i010608100.00
Molecular weight molecular_weight26996.0 kDa
Excluded volume excluded_volume34955 ų
Envelope volume envelope_volume40247 ų
Hydration-shell volume shell_volume18213 ų
Envelope diameter envelope_diameter64.9
Shell Rg shell_rg24.90
Envelope Rg envelope_rg19.29
Shape Rg shape_rg18.68
Total Rg total_rg19.74
Total atoms total_atoms1906
Residues n_residues267
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 dmax65.0
Rg (real space) rg_real19.93
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.0610e+07
I(0) uncertainty (real space) i0_real_error1.4400e+05
Rg (reciprocal space) rg_reciprocal19.93
I(0) (reciprocal space) i0_reciprocal10610000.0000
Solution quality estimate total_estimate0.6490
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis-0.282
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1888000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 0.338; Positv: 1.000; Valcen: 0.980; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)