4gng

Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3K9me3 peptide

Method: X-RAY DIFFRACTION Dmax: 85.1 Å Quality: GOOD

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

Histone-lysine N-methyltransferase NSD3

Homo sapiens

UniProt Q9BZ95

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 1310–1413 Fragment:UNP RESIDUES 1310-1413 Histone H3.3 × 1 (P84243) ZN ZINC ION × 4 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;283 K;0.1M Mes pH 6.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 283K Resolution 1.73 Å R-free 0.214
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1310–1413 Fragment:UNP RESIDUES 1310-1413 Histone H3.3 × 1 (P84243) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;283 K;0.1M Mes pH 6.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 283K Resolution 1.73 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.

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

View Construct and Data Evidence
UniProt name NSD3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–107; UniProt 1310–1413 Author chain D; PDBConstruct 4–107; UniProt 1310–1413

Histone H3.3

OrganismNot specified

UniProt P84243

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 2–16 Fragment:UNP RESIDUES 2-16 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) ZN ZINC ION × 4 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;283 K;0.1M Mes pH 6.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 283K Resolution 1.73 Å R-free 0.214
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 2–16 Fragment:UNP RESIDUES 2-16 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;283 K;0.1M Mes pH 6.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 283K Resolution 1.73 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.

94 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 2–16 Author chain F; PDBConstruct 1–15; UniProt 2–16

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 4gng

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gng
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gng
Deposition date deposition_date2012-08-17
Structure title titleCrystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3K9me3 peptide
Keywords keywordszinc finger, transcription, histone, lysine methyaltion, nuclear protein, TRANSFERASE-NUCLEAR PROTEIN complex; TRANSFERASE/NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.43
Radius of gyration Rg (electron density) rg_electron24.47
Forward intensity I(0) i013088400.00
Molecular weight molecular_weight24714.0 kDa
Excluded volume excluded_volume29726 ų
Envelope volume envelope_volume40580 ų
Hydration-shell volume shell_volume15462 ų
Envelope diameter envelope_diameter89.3
Shell Rg shell_rg28.85
Envelope Rg envelope_rg24.43
Shape Rg shape_rg24.50
Total Rg total_rg24.95
Total atoms total_atoms1682
Residues n_residues210
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 dmax85.1
Rg (real space) rg_real24.74
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real1.3090e+07
I(0) uncertainty (real space) i0_real_error1.8710e+05
Rg (reciprocal space) rg_reciprocal24.67
I(0) (reciprocal space) i0_reciprocal13090000.0000
Solution quality estimate total_estimate0.7706
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.437
Kurtosis Kurtosis kurtosis-0.675
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha740400.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.584; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.329; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4gngA00
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_id4gngD00
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)

8. Citations (1)

9. Files and Curves (10)