7czy

S protein of SARS-CoV-2 in complex bound with P5A-2F11_2B

Method: ELECTRON MICROSCOPY Dmax: 219.0 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 23 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 1-8,Immunoglobulin heavy variable 1-8,chain H of P5A-2F11_2B,Epididymis luminal protein 214,Epididymis luminal protein 214 ; × 2 (P0DP01,V9HW68) IG c168_light_IGKV4-1_IGKJ4,Immunoglobulin kappa constant × 2 (A0A5C2G1U0,P01834) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 1-8,Immunoglobulin heavy variable 1-8,chain H of P5A-2F11_2B,Epididymis luminal protein 214,Epididymis luminal protein 214 ;

Homo sapiens

UniProt P0DP01

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 23 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 20–117 Chain J; UniProt 20–117 Not recorded Spike glycoprotein × 3 (P0DTC2) IG c168_light_IGKV4-1_IGKJ4,Immunoglobulin kappa constant × 2 (A0A5C2G1U0,P01834) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 HV108_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–98; UniProt 20–117 Author chain J; PDBConstruct 1–98; UniProt 20–117

;Immunoglobulin heavy variable 1-8,Immunoglobulin heavy variable 1-8,chain H of P5A-2F11_2B,Epididymis luminal protein 214,Epididymis luminal protein 214 ;

Homo sapiens

UniProt V9HW68

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 23 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 127–470 Chain J; UniProt 127–470 Not recorded Spike glycoprotein × 3 (P0DTC2) IG c168_light_IGKV4-1_IGKJ4,Immunoglobulin kappa constant × 2 (A0A5C2G1U0,P01834) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V9HW68_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 109–452; UniProt 127–470 Author chain J; PDBConstruct 109–452; UniProt 127–470

IG c168_light_IGKV4-1_IGKJ4,Immunoglobulin kappa constant

Homo sapiens

UniProt A0A5C2G1U0

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 23 PDB declaration: heptameric(7) Consistent with protein copy count Chain K; UniProt 1–113 Chain N; UniProt 1–113 Not recorded Spike glycoprotein × 3 (P0DTC2) ;Immunoglobulin heavy variable 1-8,Immunoglobulin heavy variable 1-8,chain H of P5A-2F11_2B,Epididymis luminal protein 214,Epididymis luminal protein 214 ; × 2 (P0DP01,V9HW68) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5C2G1U0_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–113; UniProt 1–113 Author chain N; PDBConstruct 1–113; UniProt 1–113

IG c168_light_IGKV4-1_IGKJ4,Immunoglobulin kappa constant

Homo sapiens

UniProt P01834

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 23 PDB declaration: heptameric(7) Consistent with protein copy count Chain K; UniProt 1–107 Chain N; UniProt 1–107 Not recorded Spike glycoprotein × 3 (P0DTC2) ;Immunoglobulin heavy variable 1-8,Immunoglobulin heavy variable 1-8,chain H of P5A-2F11_2B,Epididymis luminal protein 214,Epididymis luminal protein 214 ; × 2 (P0DP01,V9HW68) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

44 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGKC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 114–220; UniProt 1–107 Author chain N; PDBConstruct 114–220; UniProt 1–107

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 7czy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7czy
Deposition date deposition_date2020-09-09
Structure title titleS protein of SARS-CoV-2 in complex bound with P5A-2F11_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_guinier67.38
Radius of gyration Rg (electron density) rg_electron67.55
Forward intensity I(0) i02740060000.00
Molecular weight molecular_weight442950.0 kDa
Excluded volume excluded_volume555020 ų
Envelope volume envelope_volume905810 ų
Hydration-shell volume shell_volume119770 ų
Envelope diameter envelope_diameter246.9
Shell Rg shell_rg61.83
Envelope Rg envelope_rg65.60
Shape Rg shape_rg67.54
Total Rg total_rg67.46
Total atoms total_atoms31186
Residues n_residues3880
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 dmax219.0
Rg (real space) rg_real67.59
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real2.7380e+09
I(0) uncertainty (real space) i0_real_error5.6790e+07
Rg (reciprocal space) rg_reciprocal66.16
I(0) (reciprocal space) i0_reciprocal2732000000.0000
Solution quality estimate total_estimate0.8301
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.7
Skewness Skewness skewness0.596
Kurtosis Kurtosis kurtosis-0.073
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0013
Highest regularization parameter α highest_alpha205200000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.220

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id7czyA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7czyB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7czyC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7czyH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czyH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czyJ01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czyJ02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czyK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7czyN01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)