4p1t

Crystal structure of the DBL3X-DBL4epsilon double domain from the extracellular part of VAR2CSA PfEMP1 from Plasmodium falciparum

Method: X-RAY DIFFRACTION Dmax: 95.3 Å Quality: EXCELLENT

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 A; UniProt 1215–1950 Fragment:DBL3X-DBL4epsilon double domain (UNP residues 1215-1950) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;292 K;18% PEG 3000, 100 mM Bis-Tris buffer, 300 mM sodium chloride Resolution 2.90 Å R-free 0.276

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 A; PDBConstruct 5–740; UniProt 1215–1950

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 4p1t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4p1t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4p1t
Deposition date deposition_date2014-02-27
Structure title titleCrystal structure of the DBL3X-DBL4epsilon double domain from the extracellular part of VAR2CSA PfEMP1 from Plasmodium falciparum
Keywords keywordsPfEMP1, CSA, DBL fold, membrane protein; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.27
Radius of gyration Rg (electron density) rg_electron29.48
Forward intensity I(0) i088566200.00
Molecular weight molecular_weight72147.0 kDa
Excluded volume excluded_volume89268 ų
Envelope volume envelope_volume115990 ų
Hydration-shell volume shell_volume33073 ų
Envelope diameter envelope_diameter96.1
Shell Rg shell_rg36.39
Envelope Rg envelope_rg29.51
Shape Rg shape_rg29.44
Total Rg total_rg30.23
Total atoms total_atoms5075
Residues n_residues649
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 dmax95.3
Rg (real space) rg_real30.28
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real8.8570e+07
I(0) uncertainty (real space) i0_real_error1.5740e+06
Rg (reciprocal space) rg_reciprocal30.28
I(0) (reciprocal space) i0_reciprocal88570000.0000
Solution quality estimate total_estimate0.9031
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.663
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20800000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)