5h30

Cryo-EM structure of zika virus complexed with Fab C10 at pH 6.5

Method: ELECTRON MICROSCOPY Dmax: 175.5 Å Quality: GOOD

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

structural protein E

OrganismNot specified

UniProt A0A024B7W1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 720 PDB declaration: 720-meric(720) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Chain D; UniProt 216–290 Chain E; UniProt 216–290 Chain F; UniProt 216–290 Not recorded IgG C10 heavy chain × 180 IgG C10 light chain × 180 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Chain D; UniProt 216–290 Chain E; UniProt 216–290 Chain F; UniProt 216–290 Not recorded IgG C10 heavy chain × 3 IgG C10 light chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
3 Protein heterocomplex Heteromer Protein × 60 PDB declaration: 60-meric(60) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Chain D; UniProt 216–290 Chain E; UniProt 216–290 Chain F; UniProt 216–290 Not recorded IgG C10 heavy chain × 15 IgG C10 light chain × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
4 Protein heterocomplex Heteromer Protein × 72 PDB declaration: 72-meric(72) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Chain D; UniProt 216–290 Chain E; UniProt 216–290 Chain F; UniProt 216–290 Not recorded IgG C10 heavy chain × 18 IgG C10 light chain × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
5 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Chain D; UniProt 216–290 Chain E; UniProt 216–290 Chain F; UniProt 216–290 Not recorded IgG C10 heavy chain × 3 IgG C10 light chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å
6 Protein heterocomplex Heteromer Protein × 720 PDB declaration: 720-meric(720) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Chain D; UniProt 216–290 Chain E; UniProt 216–290 Chain F; UniProt 216–290 Not recorded IgG C10 heavy chain × 180 IgG C10 light chain × 180 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

35 other PDB entries and 100 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A024B7W1_ZIKV
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–504; UniProt 291–794 Author chain B; PDBConstruct 1–504; UniProt 291–794 Author chain C; PDBConstruct 1–504; UniProt 291–794 Author chain D; PDBConstruct 1–75; UniProt 216–290 Author chain E; PDBConstruct 1–75; UniProt 216–290 Author chain F; PDBConstruct 1–75; UniProt 216–290

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 5h30

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5h30
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5h30
Deposition date deposition_date2016-10-19
Structure title titleCryo-EM structure of zika virus complexed with Fab C10 at pH 6.5
Keywords keywordsAntibody, VIRUS-IMMUNE SYSTEM complex; VIRUS/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.80
Radius of gyration Rg (electron density) rg_electron48.93
Forward intensity I(0) i0995724000.00
Molecular weight molecular_weight259690.0 kDa
Excluded volume excluded_volume317020 ų
Envelope volume envelope_volume334700 ų
Hydration-shell volume shell_volume61608 ų
Envelope diameter envelope_diameter185.6
Shell Rg shell_rg48.86
Envelope Rg envelope_rg46.27
Shape Rg shape_rg49.15
Total Rg total_rg48.92
Total atoms total_atoms59
Residues n_residues
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 dmax175.5
Rg (real space) rg_real49.06
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real9.9570e+08
I(0) uncertainty (real space) i0_real_error1.9700e+07
Rg (reciprocal space) rg_reciprocal48.80
I(0) (reciprocal space) i0_reciprocal995400000.0000
Solution quality estimate total_estimate0.8516
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.9
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis0.084
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha60530000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.747; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)