7c8j

Structural basis for cross-species recognition of COVID-19 virus spike receptor binding domain to bat ACE2

Method: X-RAY DIFFRACTION Dmax: 127.2 Å Quality: GOOD

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

Angiotensin-converting enzyme

Rhinolophus macrotis

UniProt E2DHI3

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 20–726 Not recorded SARS-CoV-2 Receptor binding domain × 1 (P0DTC2) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Succinic acid pH 7.0, 0.1 M BICINE pH 8.5, 30% v/v Polyethylene glycol monomethyl ether 550 Resolution 3.18 Å R-free 0.271

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 E2DHI3_RHIMR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–707; UniProt 20–726

SARS-CoV-2 Receptor binding domain

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 333–527 Fragment:UNP residues 333-527 Angiotensin-converting enzyme × 1 (E2DHI3) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M Succinic acid pH 7.0, 0.1 M BICINE pH 8.5, 30% v/v Polyethylene glycol monomethyl ether 550 Resolution 3.18 Å R-free 0.271

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 1–195; UniProt 333–527

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 7c8j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7c8j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7c8j
Deposition date deposition_date2020-06-01
Structure title titleStructural basis for cross-species recognition of COVID-19 virus spike receptor binding domain to bat ACE2
Keywords keywordsCOVID-19, receptor binding domain (RBD), Rhinolophus macrotis, bats, ACE2, VIRAL PROTEIN-PROTEIN BINDING complex; VIRAL PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.45
Radius of gyration Rg (electron density) rg_electron34.40
Forward intensity I(0) i0166774000.00
Molecular weight molecular_weight103770.0 kDa
Excluded volume excluded_volume129620 ų
Envelope volume envelope_volume166860 ų
Hydration-shell volume shell_volume42780 ų
Envelope diameter envelope_diameter132.6
Shell Rg shell_rg38.67
Envelope Rg envelope_rg34.76
Shape Rg shape_rg34.38
Total Rg total_rg34.79
Total atoms total_atoms7317
Residues n_residues902
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 dmax127.2
Rg (real space) rg_real34.72
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real1.6680e+08
I(0) uncertainty (real space) i0_real_error3.3690e+06
Rg (reciprocal space) rg_reciprocal34.55
I(0) (reciprocal space) i0_reciprocal166700000.0000
Solution quality estimate total_estimate0.8172
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.670
Kurtosis Kurtosis kurtosis0.336
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24240000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.603; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.904

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd7c8jb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.318 — SARS receptor-binding domain-like
Superfamily Superfamily superfamilyd.318.1 — SARS receptor-binding domain-like
Family Family familyd.318.1.1 — SARS receptor-binding domain-like

8. Citations (1)

9. Files and Curves (10)