7rks

Structure of the SARS-CoV receptor binding domain in complex with the human neutralizing antibody Fab fragment, C118

Method: X-RAY DIFFRACTION Dmax: 123.4 Å Quality: GOOD

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

Spike protein S1

Severe acute respiratory syndrome 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 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain R; UniProt 321–510 Not recorded C118 Antibody Fab Heavy Chain × 1 C118 Antibody Fab Light Chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2M sodium fluoride, 20% PEG 3,350 Resolution 2.70 Å R-free 0.247
2 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain S; UniProt 321–510 Not recorded C118 Antibody Fab Heavy Chain × 1 C118 Antibody Fab Light Chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2M sodium fluoride, 20% PEG 3,350 Resolution 2.70 Å R-free 0.247

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_SARS
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 1–190; UniProt 321–510 Author chain S; PDBConstruct 1–190; UniProt 321–510

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 7rks

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rks
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7rks
Deposition date deposition_date2021-07-22
Structure title titleStructure of the SARS-CoV receptor binding domain in complex with the human neutralizing antibody Fab fragment, C118
Keywords keywordsAntibody, Surface protein, Fab, coronavirus, fusion protein, binding domain, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.68
Radius of gyration Rg (electron density) rg_electron37.13
Forward intensity I(0) i0282181000.00
Molecular weight molecular_weight135840.0 kDa
Excluded volume excluded_volume169610 ų
Envelope volume envelope_volume230550 ų
Hydration-shell volume shell_volume51311 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg44.24
Envelope Rg envelope_rg36.06
Shape Rg shape_rg37.11
Total Rg total_rg37.64
Total atoms total_atoms9582
Residues n_residues1199
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 dmax123.4
Rg (real space) rg_real37.57
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real2.8220e+08
I(0) uncertainty (real space) i0_real_error4.3650e+06
Rg (reciprocal space) rg_reciprocal37.64
I(0) (reciprocal space) i0_reciprocal282200000.0000
Solution quality estimate total_estimate0.8958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35750000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7rksH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7rksH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7rksI01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7rksI02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)