9rwz

ZSWIM8-CUL3 complex bound to AGO2-miR-7-CYRANO

Method: ELECTRON MICROSCOPY Dmax: 240.0 Å Quality: GOOD

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

Protein argonaute-2

Homo sapiens

UniProt Q9UKV8

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 × 9 RNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain A; UniProt 2–859 Not recorded Elongin-B × 2 (Q15370) Elongin-C × 2 (Q15369) miR-7 × 1 Cullin-3 × 2 (Q13618) CYRANO trigger RNA × 1 Zinc finger SWIM domain-containing protein 8 × 2 (A7E2V4) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8;25 mM HEPES, 50 mM NaCl, 1 mM TCEP, pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

66 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AGO2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–870; UniProt 2–859

Elongin-B

Homo sapiens

UniProt Q15370

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 × 9 RNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain B; UniProt 1–118 Chain C; UniProt 1–118 Not recorded Protein argonaute-2 × 1 (Q9UKV8) Elongin-C × 2 (Q15369) miR-7 × 1 Cullin-3 × 2 (Q13618) CYRANO trigger RNA × 1 Zinc finger SWIM domain-containing protein 8 × 2 (A7E2V4) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8;25 mM HEPES, 50 mM NaCl, 1 mM TCEP, pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–118; UniProt 1–118 Author chain C; PDBConstruct 1–118; UniProt 1–118

Elongin-C

Homo sapiens

UniProt Q15369

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 × 9 RNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain D; UniProt 1–112 Chain E; UniProt 1–112 Not recorded Protein argonaute-2 × 1 (Q9UKV8) Elongin-B × 2 (Q15370) miR-7 × 1 Cullin-3 × 2 (Q13618) CYRANO trigger RNA × 1 Zinc finger SWIM domain-containing protein 8 × 2 (A7E2V4) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8;25 mM HEPES, 50 mM NaCl, 1 mM TCEP, pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–112; UniProt 1–112 Author chain E; PDBConstruct 1–112; UniProt 1–112

Cullin-3

Homo sapiens

UniProt Q13618

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 × 9 RNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain H; UniProt 1–390 Chain I; UniProt 1–390 Mutation:I342R, L346D Protein argonaute-2 × 1 (Q9UKV8) Elongin-B × 2 (Q15370) Elongin-C × 2 (Q15369) miR-7 × 1 CYRANO trigger RNA × 1 Zinc finger SWIM domain-containing protein 8 × 2 (A7E2V4) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8;25 mM HEPES, 50 mM NaCl, 1 mM TCEP, pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

29 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL3_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 1–390; UniProt 1–390 Author chain I; PDBConstruct 1–390; UniProt 1–390

Zinc finger SWIM domain-containing protein 8

Homo sapiens

UniProt A7E2V4

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 × 9 RNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain M; UniProt 1–1837 Chain N; UniProt 1–1837 Not recorded Protein argonaute-2 × 1 (Q9UKV8) Elongin-B × 2 (Q15370) Elongin-C × 2 (Q15369) miR-7 × 1 Cullin-3 × 2 (Q13618) CYRANO trigger RNA × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8;25 mM HEPES, 50 mM NaCl, 1 mM TCEP, pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ZSWM8_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–1837; UniProt 1–1837 Author chain N; PDBConstruct 1–1837; UniProt 1–1837

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 9rwz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rwz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rwz
Deposition date deposition_date2025-07-10
Structure title titleZSWIM8-CUL3 complex bound to AGO2-miR-7-CYRANO
Keywords keywordsmiRNA, E3 Ligase, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.28
Radius of gyration Rg (electron density) rg_electron68.22
Forward intensity I(0) i02534470000.00
Molecular weight molecular_weight407750.0 kDa
Excluded volume excluded_volume502880 ų
Envelope volume envelope_volume919390 ų
Hydration-shell volume shell_volume110620 ų
Envelope diameter envelope_diameter235.3
Shell Rg shell_rg71.39
Envelope Rg envelope_rg66.03
Shape Rg shape_rg68.32
Total Rg total_rg67.92
Total atoms total_atoms28601
Residues n_residues3659
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 dmax240.0
Rg (real space) rg_real68.26
Rg uncertainty (real space) rg_real_error3.12
I(0) (real space) i0_real2.5340e+09
I(0) uncertainty (real space) i0_real_error5.6520e+07
Rg (reciprocal space) rg_reciprocal68.22
I(0) (reciprocal space) i0_reciprocal2534000000.0000
Solution quality estimate total_estimate0.8730
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary83.5
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.539
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha117100000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.772

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)