3u5n

Crystal structure of the complex of TRIM33 PHD-Bromo and H3(1-20)K9me3K14ac histone peptide

Method: X-RAY DIFFRACTION Dmax: 73.7 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 882–1087 Fragment:The C-terminal PHD and Bromo dual domains of TRIM33, UNP residues 882-1087 Histone H3.1 × 1 (P68431) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M ammonium tartrate and 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.95 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 882–1087 Fragment:The C-terminal PHD and Bromo dual domains of TRIM33, UNP residues 882-1087 Histone H3.1 × 1 (P68431) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M ammonium tartrate and 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.95 Å R-free 0.256

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 33 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 2–207; UniProt 882–1087 Author chain B; PDBConstruct 2–207; UniProt 882–1087

Histone H3.1

OrganismNot specified

UniProt P68431

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 2–21 Fragment:N-terminal histone H3 peptide containing trimethylated K9 and acetylated K14, UNP residues 2-21 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase TRIM33 × 1 (Q9UPN9) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M ammonium tartrate and 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.95 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–21 Fragment:N-terminal histone H3 peptide containing trimethylated K9 and acetylated K14, UNP residues 2-21 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase TRIM33 × 1 (Q9UPN9) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M ammonium tartrate and 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.95 Å R-free 0.256

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.

402 other PDB entries and 474 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 2–21 Author chain D; PDBConstruct 1–20; UniProt 2–21

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 3u5n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3u5n
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3u5n
Deposition date deposition_date2011-10-11
Structure title titleCrystal structure of the complex of TRIM33 PHD-Bromo and H3(1-20)K9me3K14ac histone peptide
Keywords keywordsTRIM33, PHD, Bromodomain, TGF-beta, epigenetics, histone, methylation, K9me3, K14ac, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.37
Radius of gyration Rg (electron density) rg_electron23.27
Forward intensity I(0) i036964000.00
Molecular weight molecular_weight46335.0 kDa
Excluded volume excluded_volume57837 ų
Envelope volume envelope_volume73857 ų
Hydration-shell volume shell_volume26441 ų
Envelope diameter envelope_diameter75.2
Shell Rg shell_rg30.26
Envelope Rg envelope_rg22.96
Shape Rg shape_rg23.28
Total Rg total_rg24.13
Total atoms total_atoms3231
Residues n_residues398
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 dmax73.7
Rg (real space) rg_real24.22
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.6960e+07
I(0) uncertainty (real space) i0_real_error5.3840e+05
Rg (reciprocal space) rg_reciprocal24.26
I(0) (reciprocal space) i0_reciprocal36960000.0000
Solution quality estimate total_estimate0.9129
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6450000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3u5nA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id3u5nA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like
Domain ID domain_id3u5nB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id3u5nB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like

8. Citations (1)

9. Files and Curves (10)