7nnh

Cryo-EM structure of VAR2CSA FCR3 domain DBL5/6

Method: ELECTRON MICROSCOPY Dmax: 115.0 Å Quality: GOOD

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

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 1–2649 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 4.00 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 1–2649; UniProt 1–2649

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 7nnh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nnh
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7nnh
Deposition date deposition_date2021-02-24
Structure title titleCryo-EM structure of VAR2CSA FCR3 domain DBL5/6
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_guinier32.35
Radius of gyration Rg (electron density) rg_electron32.48
Forward intensity I(0) i093848600.00
Molecular weight molecular_weight75505.0 kDa
Excluded volume excluded_volume93788 ų
Envelope volume envelope_volume120220 ų
Hydration-shell volume shell_volume32749 ų
Envelope diameter envelope_diameter119.5
Shell Rg shell_rg36.87
Envelope Rg envelope_rg32.62
Shape Rg shape_rg32.43
Total Rg total_rg32.98
Total atoms total_atoms5299
Residues n_residues637
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 dmax115.0
Rg (real space) rg_real32.70
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real9.3850e+07
I(0) uncertainty (real space) i0_real_error1.7310e+06
Rg (reciprocal space) rg_reciprocal32.55
I(0) (reciprocal space) i0_reciprocal93840000.0000
Solution quality estimate total_estimate0.8311
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.586
Kurtosis Kurtosis kurtosis-0.086
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12130000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.732; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.787; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)