7kd4

Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21.

Method: X-RAY DIFFRACTION Dmax: 115.1 Å Quality: GOOD

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

Maltodextrin-binding protein and Phosphoprotein fusion protein

Menangle virus

UniProt A0A4P1LXE0

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 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–372 Mutation:C352S alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate Resolution 1.31 Å R-free 0.196
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–372 Mutation:C352S alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate Resolution 1.31 Å R-free 0.196

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.

28 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4P1LXE0_SERSF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–371; UniProt 3–372 Author chain B; PDBConstruct 2–371; UniProt 3–372

Maltodextrin-binding protein and Phosphoprotein fusion protein

Menangle virus

UniProt Q91MK1

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 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 329–388 Mutation:C352S alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate Resolution 1.31 Å R-free 0.196
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 329–388 Mutation:C352S alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate Resolution 1.31 Å R-free 0.196

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q91MK1_9MONO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 372–431; UniProt 329–388 Author chain B; PDBConstruct 372–431; UniProt 329–388

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 7kd4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kd4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kd4
Deposition date deposition_date2020-10-08
Structure title titleStructure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21.
Keywords keywordsParamyxovirus, Pararubulavirus, RNA-dependent RNA polymerase, Viral protein; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.19
Radius of gyration Rg (electron density) rg_electron34.08
Forward intensity I(0) i0142914000.00
Molecular weight molecular_weight96086.0 kDa
Excluded volume excluded_volume120280 ų
Envelope volume envelope_volume152620 ų
Hydration-shell volume shell_volume39016 ų
Envelope diameter envelope_diameter119.1
Shell Rg shell_rg38.97
Envelope Rg envelope_rg33.85
Shape Rg shape_rg34.06
Total Rg total_rg34.50
Total atoms total_atoms6754
Residues n_residues862
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 dmax115.1
Rg (real space) rg_real34.37
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real1.4290e+08
I(0) uncertainty (real space) i0_real_error2.5140e+06
Rg (reciprocal space) rg_reciprocal34.26
I(0) (reciprocal space) i0_reciprocal142900000.0000
Solution quality estimate total_estimate0.8611
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61740000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.838

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)