7eng

Cryo-EM structure of the SARS-CoV-2 S-6P in complex with Fab30 (local refinement of the RBD and Fab30)

Method: ELECTRON MICROSCOPY Dmax: 108.9 Å Quality: GOOD

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–1208 Fragment:UNP residues 1-1208 Mutation:R682G, R683S, R685S, F817P, A892P, A899P, A942P, K986P, V987P Light chain of Fab30 × 1 Heavy chain of Fab30 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–1208; UniProt 1–1208

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 7eng

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7eng
Deposition date deposition_date2021-04-16
Structure title titleCryo-EM structure of the SARS-CoV-2 S-6P in complex with Fab30 (local refinement of the RBD and Fab30)
Keywords keywordsIMMUNE SYSTEM, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.12
Radius of gyration Rg (electron density) rg_electron31.99
Forward intensity I(0) i080713800.00
Molecular weight molecular_weight70311.0 kDa
Excluded volume excluded_volume87502 ų
Envelope volume envelope_volume116510 ų
Hydration-shell volume shell_volume32338 ų
Envelope diameter envelope_diameter110.1
Shell Rg shell_rg36.85
Envelope Rg envelope_rg31.84
Shape Rg shape_rg31.96
Total Rg total_rg32.50
Total atoms total_atoms4954
Residues n_residues640
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 dmax108.9
Rg (real space) rg_real32.39
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real8.0710e+07
I(0) uncertainty (real space) i0_real_error1.2710e+06
Rg (reciprocal space) rg_reciprocal32.28
I(0) (reciprocal space) i0_reciprocal80710000.0000
Solution quality estimate total_estimate0.7908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.3
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10410000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.857; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7engH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7engH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7engL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7engL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)