7kni

Cryo-EM structure of Triple ACE2-bound SARS-CoV-2 Trimer Spike at pH 5.5

Method: ELECTRON MICROSCOPY Dmax: 206.1 Å Quality: REASONABLE

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

Spike glycoprotein

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 Other combination Heteromer Protein × 6 其他Polymer 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1208 Chain B; UniProt 1–1208 Chain C; UniProt 1–1208 Not recorded Angiotensin-converting enzyme 2 × 3 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 56 ELECTRON MICROSCOPY cryo-EM buffer:pH 5.5;PBS with NaAcetate pH 5.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1208; UniProt 1–1208 Author chain B; PDBConstruct 1–1208; UniProt 1–1208 Author chain C; PDBConstruct 1–1208; UniProt 1–1208

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 × 6 其他Polymer 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 19–615 Chain E; UniProt 19–615 Chain F; UniProt 19–615 Not recorded Spike glycoprotein × 3 (P0DTC2) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 56 ELECTRON MICROSCOPY cryo-EM buffer:pH 5.5;PBS with NaAcetate pH 5.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 E; PDBConstruct 1–597; UniProt 19–615 Author chain F; 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 7kni

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kni
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kni
Deposition date deposition_date2020-11-04
Structure title titleCryo-EM structure of Triple ACE2-bound SARS-CoV-2 Trimer Spike at pH 5.5
Keywords keywordsCOVID, COVID19, SARS-CoV2, ACE2, prefusion, 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_guinier71.52
Radius of gyration Rg (electron density) rg_electron71.38
Forward intensity I(0) i04310850000.00
Molecular weight molecular_weight561520.0 kDa
Excluded volume excluded_volume703800 ų
Envelope volume envelope_volume1153900 ų
Hydration-shell volume shell_volume139120 ų
Envelope diameter envelope_diameter237.8
Shell Rg shell_rg71.00
Envelope Rg envelope_rg67.35
Shape Rg shape_rg71.41
Total Rg total_rg71.26
Total atoms total_atoms39574
Residues n_residues4878
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 dmax206.1
Rg (real space) rg_real71.32
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real4.3070e+09
I(0) uncertainty (real space) i0_real_error8.1040e+07
Rg (reciprocal space) rg_reciprocal71.64
I(0) (reciprocal space) i0_reciprocal4312000000.0000
Solution quality estimate total_estimate0.6141
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary93.7
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0073
Highest regularization parameter α highest_alpha178600000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.981; Stabil: 1.000; Sysdev: 0.006; Positv: 1.000; Valcen: 1.000; Smooth: 0.017

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7kniA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7kniB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7kniC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain

8. Citations (1)

9. Files and Curves (10)