4gnf

Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-15

Method: X-RAY DIFFRACTION Dmax: 49.6 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1M Hepes pH 7.5, 70% v/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 283K Resolution 1.55 Å R-free 0.205

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 1
Chains and sequence ranges Author chain A; 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 C; UniProt 2–16 Fragment:UNP RESIDUES 2-16 Histone-lysine N-methyltransferase NSD3 × 1 (Q9BZ95) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1M Hepes pH 7.5, 70% v/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 283K Resolution 1.55 Å R-free 0.205

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 123 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 C; 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 4gnf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gnf
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4gnf
Deposition date deposition_date2012-08-17
Structure title titleCrystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-15
Keywords keywordszinc finger, transcription, histone, 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_guinier14.80
Radius of gyration Rg (electron density) rg_electron14.01
Forward intensity I(0) i03565880.00
Molecular weight molecular_weight12030.0 kDa
Excluded volume excluded_volume14425 ų
Envelope volume envelope_volume16901 ų
Hydration-shell volume shell_volume10516 ų
Envelope diameter envelope_diameter48.1
Shell Rg shell_rg19.14
Envelope Rg envelope_rg14.39
Shape Rg shape_rg14.01
Total Rg total_rg15.01
Total atoms total_atoms819
Residues n_residues105
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 dmax49.6
Rg (real space) rg_real14.74
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.5660e+06
I(0) uncertainty (real space) i0_real_error4.4740e+04
Rg (reciprocal space) rg_reciprocal14.75
I(0) (reciprocal space) i0_reciprocal3566000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.3
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha421700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4gnfA00
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)