7s7c

Human Nuclear Exosome Targeting (NEXT) complex bound to RNA (substrate 2)

Method: ELECTRON MICROSCOPY Dmax: 156.1 Å Quality: GOOD

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain A; UniProt 1–1042 Chain E; UniProt 1–1042 Not recorded Zinc finger CCHC domain-containing protein 8 × 2 (Q6NZY4) RNA-binding protein 7 × 1 (Q9Y580) RNA (30-MER) × 2 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;30 s wait time, blot for 2.5 s before plunging Resolution 3.62 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 A; PDBConstruct 4–1045; UniProt 1–1042 Author chain E; PDBConstruct 4–1045; 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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain B; UniProt 1–415 Chain B; UniProt 508–707 Chain F; UniProt 1–415 Chain F; UniProt 508–707 Not recorded Exosome RNA helicase MTR4 × 2 (P42285) RNA-binding protein 7 × 1 (Q9Y580) RNA (30-MER) × 2 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;30 s wait time, blot for 2.5 s before plunging Resolution 3.62 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 2
Chains and sequence ranges Author chain B; PDBConstruct 4–418; UniProt 1–415 Author chain B; PDBConstruct 419–618; UniProt 508–707 Author chain F; PDBConstruct 4–418; UniProt 1–415 Author chain F; PDBConstruct 419–618; UniProt 508–707

RNA-binding protein 7

Homo sapiens

UniProt Q9Y580

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 × 5 RNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain C; UniProt 7–86 Not recorded Exosome RNA helicase MTR4 × 2 (P42285) Zinc finger CCHC domain-containing protein 8 × 2 (Q6NZY4) RNA (30-MER) × 2 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;30 s wait time, blot for 2.5 s before plunging Resolution 3.62 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.

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

View Construct and Data Evidence
UniProt name RBM7_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–83; UniProt 7–86

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 7s7c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s7c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s7c
Deposition date deposition_date2021-09-15
Structure title titleHuman Nuclear Exosome Targeting (NEXT) complex bound to RNA (substrate 2)
Keywords keywordsHelicase, ATPase, RNA, Exosome, RNA BINDING PROTEIN, RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.15
Radius of gyration Rg (electron density) rg_electron47.58
Forward intensity I(0) i0599758000.00
Molecular weight molecular_weight197690.0 kDa
Excluded volume excluded_volume245520 ų
Envelope volume envelope_volume367510 ų
Hydration-shell volume shell_volume65544 ų
Envelope diameter envelope_diameter157.6
Shell Rg shell_rg51.24
Envelope Rg envelope_rg46.14
Shape Rg shape_rg47.56
Total Rg total_rg47.83
Total atoms total_atoms13850
Residues n_residues1666
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 dmax156.1
Rg (real space) rg_real48.16
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real5.9980e+08
I(0) uncertainty (real space) i0_real_error9.9500e+06
Rg (reciprocal space) rg_reciprocal48.15
I(0) (reciprocal space) i0_reciprocal599700000.0000
Solution quality estimate total_estimate0.8825
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.3
Skewness Skewness skewness0.217
Kurtosis Kurtosis kurtosis-0.677
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60740000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.650

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)