4o2x

Structure of a malarial protein

Method: X-RAY DIFFRACTION Dmax: 113.8 Å Quality: GOOD

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

Maltose-binding periplasmic protein, ATP-dependent Clp protease adaptor protein ClpS containing protein chimeric construct

Plasmodium falciparum (isolate 3D7)

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–371 Fragment:MBP residues, malarial ClpS residues 73-192 Mutation:A83D, A84K, A1733, A174N, A240K, A360E, A363K, A364D No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5;273 K;Ammonium Sulfate 2 M, NaCl 1.8 M no buffer, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 273K Resolution 2.70 Å R-free 0.239
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–371 Fragment:MBP residues, malarial ClpS residues 73-192 Mutation:A83D, A84K, A1733, A174N, A240K, A360E, A363K, A364D No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5;273 K;Ammonium Sulfate 2 M, NaCl 1.8 M no buffer, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 273K Resolution 2.70 Å R-free 0.239

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.

366 other PDB entries and 490 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–371; UniProt 1–371 Author chain B; PDBConstruct 1–371; UniProt 1–371

Maltose-binding periplasmic protein, ATP-dependent Clp protease adaptor protein ClpS containing protein chimeric construct

Plasmodium falciparum (isolate 3D7)

UniProt Q8IEB2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 73–192 Fragment:MBP residues, malarial ClpS residues 73-192 Mutation:A83D, A84K, A1733, A174N, A240K, A360E, A363K, A364D No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5;273 K;Ammonium Sulfate 2 M, NaCl 1.8 M no buffer, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 273K Resolution 2.70 Å R-free 0.239
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 73–192 Fragment:MBP residues, malarial ClpS residues 73-192 Mutation:A83D, A84K, A1733, A174N, A240K, A360E, A363K, A364D No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5;273 K;Ammonium Sulfate 2 M, NaCl 1.8 M no buffer, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 273K Resolution 2.70 Å R-free 0.239

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 Q8IEB2_PLAF7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 372–491; UniProt 73–192 Author chain B; PDBConstruct 372–491; UniProt 73–192

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 4o2x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4o2x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4o2x
Deposition date deposition_date2013-12-17
Structure title titleStructure of a malarial protein
Keywords keywordsClpS, Proteolysis, Clp ATPase Protease, APICOPLAST, transport protein; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.03
Radius of gyration Rg (electron density) rg_electron34.56
Forward intensity I(0) i0139016000.00
Molecular weight molecular_weight96443.0 kDa
Excluded volume excluded_volume121440 ų
Envelope volume envelope_volume159140 ų
Hydration-shell volume shell_volume39708 ų
Envelope diameter envelope_diameter115.1
Shell Rg shell_rg39.67
Envelope Rg envelope_rg33.45
Shape Rg shape_rg34.52
Total Rg total_rg35.11
Total atoms total_atoms6828
Residues n_residues911
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 dmax113.8
Rg (real space) rg_real35.06
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.3900e+08
I(0) uncertainty (real space) i0_real_error2.0630e+06
Rg (reciprocal space) rg_reciprocal35.05
I(0) (reciprocal space) i0_reciprocal139000000.0000
Solution quality estimate total_estimate0.8976
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17240000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)