7crr

Native NSD3 bound to 187-bp nucleosome

Method: ELECTRON MICROSCOPY Dmax: 169.3 Å Quality: GOOD

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

Histone H3

Xenopus laevis

UniProt Q92133

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain E; UniProt 2–136 Chain M; UniProt 2–136 Mutation:K36Nle, M90Nle, M120Nle Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (Q6AZK7) DNA (168-MER) × 1 DNA(168-MER) × 1 Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 s before being plunged into liquid ethane Resolution 3.48 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.

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q92133_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 2–136 Author chain M; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt P62799

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3 × 2 (Q92133) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (Q6AZK7) DNA (168-MER) × 1 DNA(168-MER) × 1 Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 s before being plunged into liquid ethane Resolution 3.48 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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3 × 2 (Q92133) Histone H4 × 2 (P62799) Histone H2B × 2 (Q6AZK7) DNA (168-MER) × 1 DNA(168-MER) × 1 Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 s before being plunged into liquid ethane Resolution 3.48 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.

226 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B

Xenopus tropicalis

UniProt Q6AZK7

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3 × 2 (Q92133) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (168-MER) × 1 DNA(168-MER) × 1 Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 s before being plunged into liquid ethane Resolution 3.48 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZK7_XENTR
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain I; UniProt 680–1437 Not recorded Histone H3 × 2 (Q92133) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (Q6AZK7) DNA (168-MER) × 1 DNA(168-MER) × 1 SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 s before being plunged into liquid ethane Resolution 3.48 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.

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

View Construct and Data Evidence
UniProt name NSD3_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain I; PDBConstruct 1–758; UniProt 680–1437

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 7crr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7crr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7crr
Deposition date deposition_date2020-08-14
Structure title titleNative NSD3 bound to 187-bp nucleosome
Keywords keywordsnucleosome complex, histone methyltransferase, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.71
Radius of gyration Rg (electron density) rg_electron46.25
Forward intensity I(0) i01228590000.00
Molecular weight molecular_weight217430.0 kDa
Excluded volume excluded_volume242140 ų
Envelope volume envelope_volume409490 ų
Hydration-shell volume shell_volume74541 ų
Envelope diameter envelope_diameter174.1
Shell Rg shell_rg49.87
Envelope Rg envelope_rg46.43
Shape Rg shape_rg46.09
Total Rg total_rg46.75
Total atoms total_atoms14839
Residues n_residues1333
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 dmax169.3
Rg (real space) rg_real48.82
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real1.2290e+09
I(0) uncertainty (real space) i0_real_error2.3510e+07
Rg (reciprocal space) rg_reciprocal48.71
I(0) (reciprocal space) i0_reciprocal1228000000.0000
Solution quality estimate total_estimate0.8612
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.9
Skewness Skewness skewness0.413
Kurtosis Kurtosis kurtosis-0.172
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha123600000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.790

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)