8sph

Crystal structure of chimeric omicron RBD (strain XBB.1) complexed with human ACE2

Method: X-RAY DIFFRACTION Dmax: 154.5 Å Quality: GOOD

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

Angiotensin-converting enzyme 2

Homo sapiens

UniProt Q9BYF1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 5 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–615 Fragment:UNP residues 19-615 Spike protein S1 × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ZN ZINC ION × 1 CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.2;298 K;100 mM Tris, pH 8.2, 24% PEG6000, 150 mM sodium chloride, 10% ethylene glycol Resolution 2.71 Å R-free 0.283
2 Other combination Heteromer Protein × 2 其他Polymer 4 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 19–615 Fragment:UNP residues 19-615 Spike protein S1 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.2;298 K;100 mM Tris, pH 8.2, 24% PEG6000, 150 mM sodium chloride, 10% ethylene glycol Resolution 2.71 Å R-free 0.283

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.

338 other PDB entries and 387 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–597; UniProt 19–615 Author chain B; PDBConstruct 1–597; UniProt 19–615

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 8sph

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sph
Deposition date deposition_date2023-05-03
Structure title titleCrystal structure of chimeric omicron RBD (strain XBB.1) complexed with human ACE2
Keywords keywordsSARS2, CELL INVASION, HYDROLASE-VIRAL PROTEIN complex; HYDROLASE/VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.57
Radius of gyration Rg (electron density) rg_electron45.25
Forward intensity I(0) i0508165000.00
Molecular weight molecular_weight186490.0 kDa
Excluded volume excluded_volume232850 ų
Envelope volume envelope_volume326240 ų
Hydration-shell volume shell_volume60204 ų
Envelope diameter envelope_diameter156.0
Shell Rg shell_rg49.72
Envelope Rg envelope_rg44.55
Shape Rg shape_rg45.22
Total Rg total_rg45.56
Total atoms total_atoms13133
Residues n_residues1579
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 dmax154.5
Rg (real space) rg_real45.64
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real5.0820e+08
I(0) uncertainty (real space) i0_real_error9.6870e+06
Rg (reciprocal space) rg_reciprocal45.58
I(0) (reciprocal space) i0_reciprocal508100000.0000
Solution quality estimate total_estimate0.8692
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.655
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94600000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.892; Smooth: 0.881

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)