8jwh

Cryo-EM structure of apo-state huamn angiotensin-converting enzyme 2 (ACE2)

Method: ELECTRON MICROSCOPY Dmax: 80.7 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–615 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7;The main salt in buffer should be volatile. cryo-EM vitrification conditions:Cryogen ETHANE;Vitrification carried out through ESI-cryoPrep method. Resolution 3.34 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

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 8jwh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8jwh
Deposition date deposition_date2023-06-29
Structure title titleCryo-EM structure of apo-state huamn angiotensin-converting enzyme 2 (ACE2)
Keywords keywordsReceptor, SARS-Cov-2, Viral infection, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.24
Radius of gyration Rg (electron density) rg_electron24.08
Forward intensity I(0) i077320400.00
Molecular weight molecular_weight69041.0 kDa
Excluded volume excluded_volume86217 ų
Envelope volume envelope_volume102500 ų
Hydration-shell volume shell_volume34239 ų
Envelope diameter envelope_diameter83.8
Shell Rg shell_rg32.51
Envelope Rg envelope_rg24.05
Shape Rg shape_rg24.05
Total Rg total_rg25.02
Total atoms total_atoms4870
Residues n_residues597
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 dmax80.7
Rg (real space) rg_real25.09
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real7.7320e+07
I(0) uncertainty (real space) i0_real_error9.5620e+05
Rg (reciprocal space) rg_reciprocal25.14
I(0) (reciprocal space) i0_reciprocal77320000.0000
Solution quality estimate total_estimate0.8876
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.1
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16720000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)