5gzr

Zika virus E protein complexed with a neutralizing antibody Z23-Fab

Method: ELECTRON MICROSCOPY Dmax: 209.2 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 × 600 PDB declaration: 600-meric(600) 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 Z23 Fab heavy chain × 120 Z23 Fab light chain × 120 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL Zika virus-Z23 Fab complex sample was transferred onto a glow-discharged ultra-thin carbon-coated copper grid (Purchased from Zhongjingkeyi Company, China) followed by 60s waiting and blotted for 2s with filter paper before plugging into liquid ethane using the FEI Vitrobot Mark IV Resolution 9.40 Å
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) 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 Z23 Fab heavy chain × 2 Z23 Fab light chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL Zika virus-Z23 Fab complex sample was transferred onto a glow-discharged ultra-thin carbon-coated copper grid (Purchased from Zhongjingkeyi Company, China) followed by 60s waiting and blotted for 2s with filter paper before plugging into liquid ethane using the FEI Vitrobot Mark IV Resolution 9.40 Å
3 Protein heterocomplex Heteromer Protein × 50 PDB declaration: 50-meric(50) 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 Z23 Fab heavy chain × 10 Z23 Fab light chain × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL Zika virus-Z23 Fab complex sample was transferred onto a glow-discharged ultra-thin carbon-coated copper grid (Purchased from Zhongjingkeyi Company, China) followed by 60s waiting and blotted for 2s with filter paper before plugging into liquid ethane using the FEI Vitrobot Mark IV Resolution 9.40 Å
4 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 Z23 Fab heavy chain × 12 Z23 Fab light chain × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL Zika virus-Z23 Fab complex sample was transferred onto a glow-discharged ultra-thin carbon-coated copper grid (Purchased from Zhongjingkeyi Company, China) followed by 60s waiting and blotted for 2s with filter paper before plugging into liquid ethane using the FEI Vitrobot Mark IV Resolution 9.40 Å
5 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) 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 Z23 Fab heavy chain × 2 Z23 Fab light chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL Zika virus-Z23 Fab complex sample was transferred onto a glow-discharged ultra-thin carbon-coated copper grid (Purchased from Zhongjingkeyi Company, China) followed by 60s waiting and blotted for 2s with filter paper before plugging into liquid ethane using the FEI Vitrobot Mark IV Resolution 9.40 Å
6 Protein heterocomplex Heteromer Protein × 600 PDB declaration: 600-meric(600) 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 Z23 Fab heavy chain × 120 Z23 Fab light chain × 120 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL Zika virus-Z23 Fab complex sample was transferred onto a glow-discharged ultra-thin carbon-coated copper grid (Purchased from Zhongjingkeyi Company, China) followed by 60s waiting and blotted for 2s with filter paper before plugging into liquid ethane using the FEI Vitrobot Mark IV Resolution 9.40 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 5gzr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5gzr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5gzr
Deposition date deposition_date2016-10-01
Structure title titleZika virus E protein complexed with a neutralizing antibody Z23-Fab
Keywords keywordsZika virus, Neutralizing antibody, Single Particle Reconstruction, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.19
Radius of gyration Rg (electron density) rg_electron61.01
Forward intensity I(0) i01152120000.00
Molecular weight molecular_weight281750.0 kDa
Excluded volume excluded_volume344170 ų
Envelope volume envelope_volume404630 ų
Hydration-shell volume shell_volume62594 ų
Envelope diameter envelope_diameter226.9
Shell Rg shell_rg52.71
Envelope Rg envelope_rg58.45
Shape Rg shape_rg61.30
Total Rg total_rg60.82
Total atoms total_atoms
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 dmax209.2
Rg (real space) rg_real60.89
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real1.1520e+09
I(0) uncertainty (real space) i0_real_error2.4300e+07
Rg (reciprocal space) rg_reciprocal59.57
I(0) (reciprocal space) i0_reciprocal1150000000.0000
Solution quality estimate total_estimate0.8347
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.3
Skewness Skewness skewness0.571
Kurtosis Kurtosis kurtosis-0.174
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0023
Highest regularization parameter α highest_alpha42520000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.417

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)