7b54

VAR2CSA full ectodomain in present of plCS, DBL1-DBL4

Method: ELECTRON MICROSCOPY Dmax: 141.6 Å Quality: GOOD

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

VAR2CSA in presence of plCS, DBl1-DBL4,Erythrocyte membrane protein 1

Plasmodium falciparum

UniProt Q6UDW7

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain X; UniProt 500–1985 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM Tris pH 7.5 and 75mM KCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6UDW7_PLAFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 410–1895; UniProt 500–1985

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 7b54

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7b54
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7b54
Deposition date deposition_date2020-12-03
Structure title titleVAR2CSA full ectodomain in present of plCS, DBL1-DBL4
Keywords keywordsVAR2CSA, CELL ADHESION, malaria, pfEMP1, DBL; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.85
Radius of gyration Rg (electron density) rg_electron42.65
Forward intensity I(0) i0641150000.00
Molecular weight molecular_weight201550.0 kDa
Excluded volume excluded_volume249340 ų
Envelope volume envelope_volume338420 ų
Hydration-shell volume shell_volume66628 ų
Envelope diameter envelope_diameter152.8
Shell Rg shell_rg47.24
Envelope Rg envelope_rg42.34
Shape Rg shape_rg42.62
Total Rg total_rg42.95
Total atoms total_atoms14148
Residues n_residues1732
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 dmax141.6
Rg (real space) rg_real42.91
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real6.4110e+08
I(0) uncertainty (real space) i0_real_error1.2570e+07
Rg (reciprocal space) rg_reciprocal42.85
I(0) (reciprocal space) i0_reciprocal641100000.0000
Solution quality estimate total_estimate0.8711
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.7
Skewness Skewness skewness0.397
Kurtosis Kurtosis kurtosis-0.236
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98860000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.670

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)