8wlz

Cryo-EM structure of the WIV1 S-hACE2 complex

Method: ELECTRON MICROSCOPY Dmax: 208.3 Å Quality: GOOD

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

Spike glycoprotein,Fibritin

Enterobacteria phage T6

UniProt A0A346FJN8

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 × 5 其他Polymer 16 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 458–483 Chain B; UniProt 458–483 Chain C; UniProt 458–483 Not recorded Processed angiotensin-converting enzyme 2 × 2 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 13 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.45 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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A346FJN8_BPT6
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1194–1219; UniProt 458–483 Author chain B; PDBConstruct 1194–1219; UniProt 458–483 Author chain C; PDBConstruct 1194–1219; UniProt 458–483

Spike glycoprotein,Fibritin

Enterobacteria phage T6

UniProt U5WI05

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 × 5 其他Polymer 16 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–1191 Chain B; UniProt 1–1191 Chain C; UniProt 1–1191 Not recorded Processed angiotensin-converting enzyme 2 × 2 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 13 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.45 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name U5WI05_SARS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1191; UniProt 1–1191 Author chain B; PDBConstruct 1–1191; UniProt 1–1191 Author chain C; PDBConstruct 1–1191; UniProt 1–1191

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 Insufficient information Heteromer Protein × 5 其他Polymer 16 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 19–615 Chain G; UniProt 19–615 Not recorded Spike glycoprotein,Fibritin × 3 (U5WI05,A0A346FJN8) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 13 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.45 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 2
Chains and sequence ranges Author chain D; PDBConstruct 1–597; UniProt 19–615 Author chain G; 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 8wlz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wlz
Deposition date deposition_date2023-10-01
Structure title titleCryo-EM structure of the WIV1 S-hACE2 complex
Keywords keywordsspike, 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_guinier69.99
Radius of gyration Rg (electron density) rg_electron70.14
Forward intensity I(0) i03510990000.00
Molecular weight molecular_weight503810.0 kDa
Excluded volume excluded_volume630820 ų
Envelope volume envelope_volume989050 ų
Hydration-shell volume shell_volume124000 ų
Envelope diameter envelope_diameter234.4
Shell Rg shell_rg65.85
Envelope Rg envelope_rg66.97
Shape Rg shape_rg70.17
Total Rg total_rg69.94
Total atoms total_atoms35498
Residues n_residues4397
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 dmax208.3
Rg (real space) rg_real69.95
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real3.5080e+09
I(0) uncertainty (real space) i0_real_error7.2770e+07
Rg (reciprocal space) rg_reciprocal69.65
I(0) (reciprocal space) i0_reciprocal3508000000.0000
Solution quality estimate total_estimate0.8451
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary94.7
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0054
Highest regularization parameter α highest_alpha160000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.989; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.015

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)