9yc3

Crystal structure of malaria transmission-blocking antigen PfHAP2 domain 3 in complex with nanobody WNb 334

Method: X-RAY DIFFRACTION Dmax: 63.6 Å Quality: GOOD

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

Male gamete fusion factor HAP2

Plasmodium falciparum

UniProt Q8IJQ3

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 500–620 Not recorded Nanobody WNb 334 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.7;293 K;0.1 M HEPES pH 7.7, 27% w/v PEG 3350 Resolution 2.80 Å R-free 0.253

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 Q8IJQ3_PLAF7
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–123; UniProt 500–620

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 9yc3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yc3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yc3
Deposition date deposition_date2025-09-18
Structure title titleCrystal structure of malaria transmission-blocking antigen PfHAP2 domain 3 in complex with nanobody WNb 334
Keywords keywordsTransmission-blocking, Nanobody, Fusogen, Malaria, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.42
Radius of gyration Rg (electron density) rg_electron18.30
Forward intensity I(0) i012563600.00
Molecular weight molecular_weight25448.0 kDa
Excluded volume excluded_volume31334 ų
Envelope volume envelope_volume37114 ų
Hydration-shell volume shell_volume17216 ų
Envelope diameter envelope_diameter63.2
Shell Rg shell_rg24.14
Envelope Rg envelope_rg18.51
Shape Rg shape_rg18.31
Total Rg total_rg19.13
Total atoms total_atoms1786
Residues n_residues245
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 dmax63.6
Rg (real space) rg_real19.34
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.2560e+07
I(0) uncertainty (real space) i0_real_error1.7370e+05
Rg (reciprocal space) rg_reciprocal19.35
I(0) (reciprocal space) i0_reciprocal12560000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.185
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3075000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)