7rxp

Fab1512 in complex with the C-terminal alpha-TSR domain of P. falciparum

Method: X-RAY DIFFRACTION Dmax: 92.8 Å Quality: GOOD

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

Circumsporozoite protein

Plasmodium falciparum (isolate 3D7)

UniProt Q7K740

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 A; UniProt 309–375 Fragment:C-terminal alpha-TSR domain (UNP residues 309-375) Fab1512 light chain × 1 Fab1512 heavy chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;20% PEG3000, 0.2 M sodium chloride, 0.1 M HEPES. pH 7.5 Resolution 1.76 Å R-free 0.205

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.

30 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7K740_PLAF7
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–67; UniProt 309–375

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 7rxp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7rxp
Deposition date deposition_date2021-08-23
Structure title titleFab1512 in complex with the C-terminal alpha-TSR domain of P. falciparum
Keywords keywordsMalaria, Antibody, Sporozoite, Circumsporozoite protein, alpha-TSR domain, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.70
Radius of gyration Rg (electron density) rg_electron27.07
Forward intensity I(0) i053697000.00
Molecular weight molecular_weight55829.0 kDa
Excluded volume excluded_volume69267 ų
Envelope volume envelope_volume87451 ų
Hydration-shell volume shell_volume27823 ų
Envelope diameter envelope_diameter94.8
Shell Rg shell_rg33.50
Envelope Rg envelope_rg26.97
Shape Rg shape_rg27.02
Total Rg total_rg27.85
Total atoms total_atoms7741
Residues n_residues495
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 dmax92.8
Rg (real space) rg_real27.81
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real5.3700e+07
I(0) uncertainty (real space) i0_real_error8.2480e+05
Rg (reciprocal space) rg_reciprocal27.78
I(0) (reciprocal space) i0_reciprocal53700000.0000
Solution quality estimate total_estimate0.8807
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.424
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha10320000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id7rxpA01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology100 — TSP-1 type 1 repeat
Homologous superfamily homologous superfamily10 — Thrombospondin type-1 (TSP1) repeat
Domain ID domain_id7rxpH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7rxpH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7rxpL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7rxpL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)