7ddo

Cryo-EM structure of human ACE2 and GD/1/2019 RBD

Method: ELECTRON MICROSCOPY Dmax: 109.8 Å Quality: REASONABLE

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–615 Not recorded Spike protein S1 × 1 (A0A6M3G9R1) ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 Resolution 3.40 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 1–597; UniProt 19–615

Spike protein S1

Pangolin coronavirus

UniProt A0A6M3G9R1

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 C; UniProt 315–523 Not recorded Angiotensin-converting enzyme 2 × 1 (Q9BYF1) ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 Resolution 3.40 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6M3G9R1_9BETC
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–209; UniProt 315–523

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 7ddo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7ddo
Deposition date deposition_date2020-10-29
Structure title titleCryo-EM structure of human ACE2 and GD/1/2019 RBD
Keywords keywordsPangolin, RBD, ACE2, PROTEIN BINDING, HYDROLASE-VIRAL PROTEIN complex; HYDROLASE/VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.38
Radius of gyration Rg (electron density) rg_electron30.86
Forward intensity I(0) i0133169000.00
Molecular weight molecular_weight91641.0 kDa
Excluded volume excluded_volume114350 ų
Envelope volume envelope_volume147000 ų
Hydration-shell volume shell_volume40444 ų
Envelope diameter envelope_diameter116.9
Shell Rg shell_rg37.37
Envelope Rg envelope_rg30.85
Shape Rg shape_rg30.83
Total Rg total_rg31.51
Total atoms total_atoms6461
Residues n_residues791
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 dmax109.8
Rg (real space) rg_real31.46
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.3320e+08
I(0) uncertainty (real space) i0_real_error2.0170e+06
Rg (reciprocal space) rg_reciprocal31.43
I(0) (reciprocal space) i0_reciprocal133200000.0000
Solution quality estimate total_estimate0.6595
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.487
Kurtosis Kurtosis kurtosis0.006
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29280000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 0.169; Positv: 1.000; Valcen: 0.990; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)