9pll

TRIM21-NUP98 Molecular Glue Complex (MAN-056)

Method: X-RAY DIFFRACTION Dmax: 81.5 Å Quality: GOOD

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

E3 ubiquitin-protein ligase TRIM21

Homo sapiens

UniProt P19474

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 284–465 Not recorded Isoform 2 of Nuclear pore complex protein Nup98-Nup96 × 1 (P52948) A1BLD (3P)-3-(4-chloro-2-ethoxyphenyl)-6-fluoro-2-[(piperazin-1-yl)methyl]quinazolin-4(3H)-one × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;100 mM NaCl, 100 mM HEPES, pH 7.5, 12 % polyethylene glycol 20,000 Resolution 1.60 Å R-free 0.214

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.

19 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RO52_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 3–184; UniProt 284–465

Isoform 2 of Nuclear pore complex protein Nup98-Nup96

Homo sapiens

UniProt P52948

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 712–863 Not recorded E3 ubiquitin-protein ligase TRIM21 × 1 (P19474) A1BLD (3P)-3-(4-chloro-2-ethoxyphenyl)-6-fluoro-2-[(piperazin-1-yl)methyl]quinazolin-4(3H)-one × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;100 mM NaCl, 100 mM HEPES, pH 7.5, 12 % polyethylene glycol 20,000 Resolution 1.60 Å R-free 0.214

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.

20 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP98_HUMAN
Isoform P52948-2
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 20–171; UniProt 712–863

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 9pll

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pll
Deposition date deposition_date2025-07-15
最后修订 last_revision2026-05-27
Structure title titleTRIM21-NUP98 Molecular Glue Complex (MAN-056)
Keywords keywordsMolecular glue, ubiquitin ligase, targeted protein degradation, nuclear pore, TRIM21, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.20
Radius of gyration Rg (electron density) rg_electron22.32
Forward intensity I(0) i046822100.00
Molecular weight molecular_weight35667.0 kDa
Excluded volume excluded_volume34576 ų
Envelope volume envelope_volume57577 ų
Hydration-shell volume shell_volume21957 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg28.58
Envelope Rg envelope_rg22.63
Shape Rg shape_rg22.28
Total Rg total_rg22.97
Total atoms total_atoms2706
Residues n_residues335
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 dmax81.5
Rg (real space) rg_real23.20
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real4.6820e+07
I(0) uncertainty (real space) i0_real_error6.8580e+05
Rg (reciprocal space) rg_reciprocal23.20
I(0) (reciprocal space) i0_reciprocal46820000.0000
Solution quality estimate total_estimate0.7879
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.379
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6345000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.770; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.928; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)