7d00

S protein of SARS-CoV-2 in complex bound with FabP5A-1B8

Method: ELECTRON MICROSCOPY Dmax: 212.5 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 IG c642_heavy_IGHV3-53_IGHD1-26_IGHJ6,chain H of FabP5A-1B8,IGH@ protein × 2 (A0A5C2GF00,Q6GMX6) IGL c4203_light_IGKV1-9_IGKJ4,Uncharacterized protein × 2 (A0A5C2GCZ2,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 3.00 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

IG c642_heavy_IGHV3-53_IGHD1-26_IGHJ6,chain H of FabP5A-1B8,IGH@ protein

Homo sapiens

UniProt A0A5C2GF00

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 1–96 Chain J; UniProt 1–96 Not recorded Spike glycoprotein × 3 (P0DTC2) IGL c4203_light_IGKV1-9_IGKJ4,Uncharacterized protein × 2 (A0A5C2GCZ2,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 3.00 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 A0A5C2GF00_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–96; UniProt 1–96 Author chain J; PDBConstruct 1–96; UniProt 1–96

IG c642_heavy_IGHV3-53_IGHD1-26_IGHJ6,chain H of FabP5A-1B8,IGH@ protein

Homo sapiens

UniProt Q6GMX6

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 123–465 Chain J; UniProt 123–465 Not recorded Spike glycoprotein × 3 (P0DTC2) IGL c4203_light_IGKV1-9_IGKJ4,Uncharacterized protein × 2 (A0A5C2GCZ2,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 3.00 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.

18 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6GMX6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 103–445; UniProt 123–465 Author chain J; PDBConstruct 103–445; UniProt 123–465

IGL c4203_light_IGKV1-9_IGKJ4,Uncharacterized protein

Homo sapiens

UniProt A0A5C2GCZ2

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 1–105 Chain N; UniProt 1–105 Not recorded Spike glycoprotein × 3 (P0DTC2) IG c642_heavy_IGHV3-53_IGHD1-26_IGHJ6,chain H of FabP5A-1B8,IGH@ protein × 2 (A0A5C2GF00,Q6GMX6) 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 3.00 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 A0A5C2GCZ2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–104; UniProt 1–105 Author chain N; PDBConstruct 1–104; UniProt 1–105

IGL c4203_light_IGKV1-9_IGKJ4,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 130–239 Chain N; UniProt 130–239 Not recorded Spike glycoprotein × 3 (P0DTC2) IG c642_heavy_IGHV3-53_IGHD1-26_IGHJ6,chain H of FabP5A-1B8,IGH@ protein × 2 (A0A5C2GF00,Q6GMX6) 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 3.00 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 105–214; UniProt 130–239 Author chain N; PDBConstruct 105–214; UniProt 130–239

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 7d00

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d00
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d00
Deposition date deposition_date2020-09-09
Structure title titleS protein of SARS-CoV-2 in complex bound with FabP5A-1B8
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_guinier64.90
Radius of gyration Rg (electron density) rg_electron65.37
Forward intensity I(0) i02678310000.00
Molecular weight molecular_weight438570.0 kDa
Excluded volume excluded_volume549880 ų
Envelope volume envelope_volume877440 ų
Hydration-shell volume shell_volume118500 ų
Envelope diameter envelope_diameter237.2
Shell Rg shell_rg61.25
Envelope Rg envelope_rg63.79
Shape Rg shape_rg65.37
Total Rg total_rg65.28
Total atoms total_atoms30886
Residues n_residues3854
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 dmax212.5
Rg (real space) rg_real65.42
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real2.6770e+09
I(0) uncertainty (real space) i0_real_error5.2920e+07
Rg (reciprocal space) rg_reciprocal64.36
I(0) (reciprocal space) i0_reciprocal2673000000.0000
Solution quality estimate total_estimate0.8405
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.8
Skewness Skewness skewness0.579
Kurtosis Kurtosis kurtosis-0.021
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0018
Highest regularization parameter α highest_alpha181700000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.324

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd7d00k1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd7d00k2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd7d00n1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd7d00n2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (11 domains)

Domain ID domain_id7d00A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7d00B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7d00C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7d00H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00J01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00J02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00K01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00K02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00N01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7d00N02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)