3scj

Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human receptor ACE2

Method: X-RAY DIFFRACTION Dmax: 151.1 Å Quality: GOOD

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 Fragment:UNP residues 19-615 Spike glycoprotein × 1 (P59594) ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;295 K;100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K Resolution 3.00 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 19–615 Fragment:UNP residues 19-615 Spike glycoprotein × 1 (P59594) ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;295 K;100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K Resolution 3.00 Å R-free 0.278

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 387 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 Author chain B; PDBConstruct 1–597; UniProt 19–615

Spike glycoprotein

SARS coronavirus

UniProt P59594

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 E; UniProt 323–502 Fragment:receptor binding domain (UNP residues 323-502) Angiotensin-converting enzyme 2 × 1 (Q9BYF1) ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;295 K;100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K Resolution 3.00 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 323–502 Fragment:receptor binding domain (UNP residues 323-502) Angiotensin-converting enzyme 2 × 1 (Q9BYF1) ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 8.5;295 K;100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K Resolution 3.00 Å R-free 0.278

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.

76 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_CVHSA
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–180; UniProt 323–502 Author chain F; PDBConstruct 1–180; UniProt 323–502

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 3scj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3scj
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3scj
Deposition date deposition_date2011-06-07
Structure title titleCrystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human receptor ACE2
Keywords keywordsbeta-sheet, HYDROLASE-VIRAL PROTEIN complex; HYDROLASE/VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.49
Radius of gyration Rg (electron density) rg_electron45.26
Forward intensity I(0) i0457838000.00
Molecular weight molecular_weight177840.0 kDa
Excluded volume excluded_volume222300 ų
Envelope volume envelope_volume311630 ų
Hydration-shell volume shell_volume57088 ų
Envelope diameter envelope_diameter154.8
Shell Rg shell_rg50.04
Envelope Rg envelope_rg44.49
Shape Rg shape_rg45.24
Total Rg total_rg45.51
Total atoms total_atoms12544
Residues n_residues1542
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 dmax151.1
Rg (real space) rg_real45.55
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real4.5780e+08
I(0) uncertainty (real space) i0_real_error8.3810e+06
Rg (reciprocal space) rg_reciprocal45.49
I(0) (reciprocal space) i0_reciprocal457800000.0000
Solution quality estimate total_estimate0.8702
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.732
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76720000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.906; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3scja_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.92 — Zincin-like
Superfamily Superfamily superfamilyd.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family familyd.92.1.5 — Neurolysin-like
Domain ID domain_idd3scjb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.92 — Zincin-like
Superfamily Superfamily superfamilyd.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family familyd.92.1.5 — Neurolysin-like
Domain ID domain_idd3scje_
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
Domain ID domain_idd3scjf_
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

CATH v4.4 (2 domains)

Domain ID domain_id3scjE01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1840 — Spike protein, C-terminal core receptor binding subdomain
Domain ID domain_id3scjF01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1840 — Spike protein, C-terminal core receptor binding subdomain

8. Citations (1)

9. Files and Curves (10)