7z52

Human NEXT dimer - focused reconstruction of the single MTR4

Method: ELECTRON MICROSCOPY Dmax: 81.8 Å Quality: EXCELLENT

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

Exosome RNA helicase MTR4

Homo sapiens

UniProt P42285

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–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 1–1042 Not recorded ;RNA (5'-R(P*UP*UP*UP*UP*U)-3') ; × 1 Zinc finger CCHC domain-containing protein 8 × 1 (Q6NZY4) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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.

10 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTREX_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 5–1046; UniProt 1–1042

Zinc finger CCHC domain-containing protein 8

Homo sapiens

UniProt Q6NZY4

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–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1–707 Not recorded Exosome RNA helicase MTR4 × 1 (P42285) ;RNA (5'-R(P*UP*UP*UP*UP*U)-3') ; × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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.

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZCHC8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 3–709; UniProt 1–707

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 7z52

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z52
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7z52
Deposition date deposition_date2022-03-07
Structure title titleHuman NEXT dimer - focused reconstruction of the single MTR4
Keywords keywordsHELICASE, ATPASE, RNA DEGRADATION, EXOSOME, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.23
Radius of gyration Rg (electron density) rg_electron27.06
Forward intensity I(0) i0118759000.00
Molecular weight molecular_weight84408.0 kDa
Excluded volume excluded_volume105200 ų
Envelope volume envelope_volume135210 ų
Hydration-shell volume shell_volume39967 ų
Envelope diameter envelope_diameter86.6
Shell Rg shell_rg35.85
Envelope Rg envelope_rg27.09
Shape Rg shape_rg27.06
Total Rg total_rg27.93
Total atoms total_atoms5911
Residues n_residues751
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 dmax81.8
Rg (real space) rg_real28.02
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.1880e+08
I(0) uncertainty (real space) i0_real_error1.4470e+06
Rg (reciprocal space) rg_reciprocal28.09
I(0) (reciprocal space) i0_reciprocal118800000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30220000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.977; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)