7czu

S protein of SARS-CoV-2 in complex bound with P5A-1B6_2B

Method: ELECTRON MICROSCOPY Dmax: 209.2 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 Insufficient information Heteromer Protein × 7 其他Polymer 21 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–1273 Chain B; UniProt 1–1273 Chain C; UniProt 1–1273 Not recorded ;Immunoglobulin heavy variable 3-30-3,Immunoglobulin heavy variable 3-30-3,Chain H of P5A-1B6_2B,Immunoglobulin gamma-1 heavy chain,Immunoglobulin gamma-1 heavy chain ; × 2 (P0DP02,P0DOX5) Immunoglobulin kappa variable 1-33,Immunoglobulin kappa variable 1-33,Uncharacterized protein × 2 (P01594,Q8TCD0) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1273; UniProt 1–1273 Author chain B; PDBConstruct 1–1273; UniProt 1–1273 Author chain C; PDBConstruct 1–1273; UniProt 1–1273

;Immunoglobulin heavy variable 3-30-3,Immunoglobulin heavy variable 3-30-3,Chain H of P5A-1B6_2B,Immunoglobulin gamma-1 heavy chain,Immunoglobulin gamma-1 heavy chain ;

Homo sapiens

UniProt P0DOX5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 其他Polymer 21 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 109–449 Chain J; UniProt 109–449 Not recorded Spike glycoprotein × 3 (P0DTC2) Immunoglobulin kappa variable 1-33,Immunoglobulin kappa variable 1-33,Uncharacterized protein × 2 (P01594,Q8TCD0) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 117–457; UniProt 109–449 Author chain J; PDBConstruct 117–457; UniProt 109–449

;Immunoglobulin heavy variable 3-30-3,Immunoglobulin heavy variable 3-30-3,Chain H of P5A-1B6_2B,Immunoglobulin gamma-1 heavy chain,Immunoglobulin gamma-1 heavy chain ;

Homo sapiens

UniProt P0DP02

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 其他Polymer 21 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 20–116 Chain J; UniProt 20–116 Not recorded Spike glycoprotein × 3 (P0DTC2) Immunoglobulin kappa variable 1-33,Immunoglobulin kappa variable 1-33,Uncharacterized protein × 2 (P01594,Q8TCD0) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HVC33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–97; UniProt 20–116 Author chain J; PDBConstruct 1–97; UniProt 20–116

Immunoglobulin kappa variable 1-33,Immunoglobulin kappa variable 1-33,Uncharacterized protein

Homo sapiens

UniProt P01594

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 其他Polymer 21 PDB declaration: heptameric(7) Consistent with protein copy count Chain K; UniProt 23–117 Chain N; UniProt 23–117 Not recorded Spike glycoprotein × 3 (P0DTC2) ;Immunoglobulin heavy variable 3-30-3,Immunoglobulin heavy variable 3-30-3,Chain H of P5A-1B6_2B,Immunoglobulin gamma-1 heavy chain,Immunoglobulin gamma-1 heavy chain ; × 2 (P0DP02,P0DOX5) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KV133_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–95; UniProt 23–117 Author chain N; PDBConstruct 1–95; UniProt 23–117

Immunoglobulin kappa variable 1-33,Immunoglobulin kappa variable 1-33,Uncharacterized protein

Homo sapiens

UniProt Q8TCD0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 其他Polymer 21 PDB declaration: heptameric(7) Consistent with protein copy count Chain K; UniProt 122–239 Chain N; UniProt 122–239 Not recorded Spike glycoprotein × 3 (P0DTC2) ;Immunoglobulin heavy variable 3-30-3,Immunoglobulin heavy variable 3-30-3,Chain H of P5A-1B6_2B,Immunoglobulin gamma-1 heavy chain,Immunoglobulin gamma-1 heavy chain ; × 2 (P0DP02,P0DOX5) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

39 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8TCD0_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 97–214; UniProt 122–239 Author chain N; PDBConstruct 97–214; UniProt 122–239

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 7czu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7czu
Deposition date deposition_date2020-09-09
Structure title titleS protein of SARS-CoV-2 in complex bound with P5A-1B6_2B
Keywords keywordsSARS-CoV-2, antibody, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.83
Radius of gyration Rg (electron density) rg_electron65.18
Forward intensity I(0) i02730080000.00
Molecular weight molecular_weight441940.0 kDa
Excluded volume excluded_volume553710 ų
Envelope volume envelope_volume887800 ų
Hydration-shell volume shell_volume119520 ų
Envelope diameter envelope_diameter235.4
Shell Rg shell_rg61.58
Envelope Rg envelope_rg63.38
Shape Rg shape_rg65.18
Total Rg total_rg65.11
Total atoms total_atoms31120
Residues n_residues3878
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 dmax209.2
Rg (real space) rg_real65.29
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real2.7290e+09
I(0) uncertainty (real space) i0_real_error5.4330e+07
Rg (reciprocal space) rg_reciprocal64.36
I(0) (reciprocal space) i0_reciprocal2725000000.0000
Solution quality estimate total_estimate0.8373
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary69.7
Skewness Skewness skewness0.548
Kurtosis Kurtosis kurtosis-0.079
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0008
Highest regularization parameter α highest_alpha168100000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.230

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 11 domains

CATH v4.4 (11 domains)

Domain ID domain_id7czuA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7czuB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7czuC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7czuH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuJ01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuJ02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuK02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuN01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czuN02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)