8bd9

Crystal structure of TRIM33 alpha PHD-Bromo domain in complex with 10

Method: X-RAY DIFFRACTION Dmax: 68.5 Å Quality: GOOD

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

E3 ubiquitin-protein ligase TRIM33

Homo sapiens

UniProt Q9UPN9

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 882–1087 Not recorded QCU 1,3-dimethylbenzimidazol-2-one × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;281 K;0.2 M calcium chloride and 20 % wt/vol PEG-3350 Resolution 3.20 Å R-free 0.349

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.

8 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRI33_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–209; UniProt 882–1087

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 8bd9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bd9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bd9
Deposition date deposition_date2022-10-18
Structure title titleCrystal structure of TRIM33 alpha PHD-Bromo domain in complex with 10
Keywords keywordsTRIM33 alpha, PHD-Bromo domain, complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.10
Radius of gyration Rg (electron density) rg_electron17.28
Forward intensity I(0) i07735820.00
Molecular weight molecular_weight20046.0 kDa
Excluded volume excluded_volume24849 ų
Envelope volume envelope_volume29563 ų
Hydration-shell volume shell_volume14905 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg22.97
Envelope Rg envelope_rg17.94
Shape Rg shape_rg17.28
Total Rg total_rg18.24
Total atoms total_atoms1399
Residues n_residues184
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 dmax68.5
Rg (real space) rg_real18.13
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real7.7360e+06
I(0) uncertainty (real space) i0_real_error9.9620e+04
Rg (reciprocal space) rg_reciprocal18.12
I(0) (reciprocal space) i0_reciprocal7736000.0000
Solution quality estimate total_estimate0.8087
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis0.135
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1512000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.542; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.886; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)