9yio

Crystal structure of 5B3 Fab in complex with PvRipr EGF7-8

Method: X-RAY DIFFRACTION Dmax: 97.5 Å Quality: GOOD

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

PvRipr EGF7-8

Plasmodium vivax

UniProt A0A564ZTL5

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 764–843 Mutation:N767Q, N780Q 5B3 kappa chain × 1 5B3 heavy chain × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;295 K;0.2M (NH4)2SO4, 20% PEG-3,350 and 0.1M Sodium Acetate buffer pH 4.4 Resolution 2.08 Å R-free 0.235

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A564ZTL5_PLAVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 4–83; UniProt 764–843

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 9yio

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yio
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yio
Deposition date deposition_date2025-10-02
Structure title titleCrystal structure of 5B3 Fab in complex with PvRipr EGF7-8
Keywords keywordsPlasmodium vivax, invasion, antibody-antigen complex, CELL INVASION; CELL INVASION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.45
Radius of gyration Rg (electron density) rg_electron28.16
Forward intensity I(0) i055144200.00
Molecular weight molecular_weight56631.0 kDa
Excluded volume excluded_volume70229 ų
Envelope volume envelope_volume90335 ų
Hydration-shell volume shell_volume28200 ų
Envelope diameter envelope_diameter102.8
Shell Rg shell_rg33.69
Envelope Rg envelope_rg28.24
Shape Rg shape_rg28.07
Total Rg total_rg28.98
Total atoms total_atoms3970
Residues n_residues506
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 dmax97.5
Rg (real space) rg_real28.64
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real5.5140e+07
I(0) uncertainty (real space) i0_real_error8.9980e+05
Rg (reciprocal space) rg_reciprocal28.58
I(0) (reciprocal space) i0_reciprocal55140000.0000
Solution quality estimate total_estimate0.8667
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.497
Kurtosis Kurtosis kurtosis-0.175
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7298000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)