7kd5

Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P212121

Method: X-RAY DIFFRACTION Dmax: 85.6 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 EDO 1,2-ETHANEDIOL × 4 PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) × 3 PRO PROLINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.7;291.15 K;20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, Crystals were transferred into the following cryo-protective solution before vitrification: 20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, 5mM Maltose, 20%(v/v) Ethylene Glycol Resolution 1.55 Å R-free 0.189

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 47 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

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 EDO 1,2-ETHANEDIOL × 4 PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) × 3 PRO PROLINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.7;291.15 K;20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, Crystals were transferred into the following cryo-protective solution before vitrification: 20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, 5mM Maltose, 20%(v/v) Ethylene Glycol Resolution 1.55 Å R-free 0.189

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 3 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

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 7kd5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kd5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kd5
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 P212121
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_guinier23.79
Radius of gyration Rg (electron density) rg_electron22.64
Forward intensity I(0) i037691200.00
Molecular weight molecular_weight48285.0 kDa
Excluded volume excluded_volume60847 ų
Envelope volume envelope_volume71907 ų
Hydration-shell volume shell_volume26250 ų
Envelope diameter envelope_diameter81.9
Shell Rg shell_rg29.92
Envelope Rg envelope_rg22.96
Shape Rg shape_rg22.56
Total Rg total_rg23.77
Total atoms total_atoms3398
Residues n_residues428
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 dmax85.6
Rg (real space) rg_real23.72
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real3.7690e+07
I(0) uncertainty (real space) i0_real_error5.9350e+05
Rg (reciprocal space) rg_reciprocal23.73
I(0) (reciprocal space) i0_reciprocal37690000.0000
Solution quality estimate total_estimate0.7727
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha10490000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.696; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7kd5A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)