8wrl

XBB.1.5 RBD in complex with ACE2

Method: ELECTRON MICROSCOPY Dmax: 108.2 Å Quality: REASONABLE

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

Processed 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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–612 Not recorded Spike protein S1 × 1 (P0DTC2) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

338 other PDB entries and 388 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 1–594; UniProt 19–612

Spike protein S1

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC2

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 319–537 Fragment:RBD domain Processed angiotensin-converting enzyme 2 × 1 (Q9BYF1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 20–238; UniProt 319–537

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 8wrl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wrl
Deposition date deposition_date2023-10-15
Structure title titleXBB.1.5 RBD in complex with ACE2
Keywords keywordsSARS-CoV-2, XBB.1.5, ACE2, RBD, VIRAL PROTEIN/HYDROLASE, VIRAL PROTEIN-HYDROLASE complex; VIRAL PROTEIN/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.40
Radius of gyration Rg (electron density) rg_electron30.95
Forward intensity I(0) i0132026000.00
Molecular weight molecular_weight91749.0 kDa
Excluded volume excluded_volume114740 ų
Envelope volume envelope_volume148760 ų
Hydration-shell volume shell_volume40799 ų
Envelope diameter envelope_diameter114.0
Shell Rg shell_rg37.47
Envelope Rg envelope_rg31.07
Shape Rg shape_rg30.91
Total Rg total_rg31.63
Total atoms total_atoms6473
Residues n_residues790
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 dmax108.2
Rg (real space) rg_real31.48
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.3200e+08
I(0) uncertainty (real space) i0_real_error2.0210e+06
Rg (reciprocal space) rg_reciprocal31.45
I(0) (reciprocal space) i0_reciprocal132000000.0000
Solution quality estimate total_estimate0.6372
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.0
Skewness Skewness skewness0.499
Kurtosis Kurtosis kurtosis0.033
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29450000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.740; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.994; Smooth: 0.881

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)