5hq2

Structural model of Set8 histone H4 Lys20 methyltransferase bound to nucleosome core particle

Method: X-RAY DIFFRACTION Dmax: 118.3 Å Quality: GOOD

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 × 12 DNA 4 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain A; UniProt 2–136 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 2 DNA (149-MER) × 2 Guanine nucleotide exchange factor SRM1 × 2 (P21827) N-lysine methyltransferase SETD8 × 2 (Q9NQR1) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 5.5;277 K;25 mM sodium acetate pH 5.5, 40 mM sodium citrate,1 mM DTT, 6% PEG2000-MME Resolution 4.50 Å R-free 0.397

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.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; 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 × 12 DNA 4 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain B; UniProt 2–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 2 DNA (149-MER) × 2 Guanine nucleotide exchange factor SRM1 × 2 (P21827) N-lysine methyltransferase SETD8 × 2 (Q9NQR1) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 5.5;277 K;25 mM sodium acetate pH 5.5, 40 mM sodium citrate,1 mM DTT, 6% PEG2000-MME Resolution 4.50 Å R-free 0.397

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

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 × 12 DNA 4 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain G; UniProt 2–130 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 2 DNA (149-MER) × 2 Guanine nucleotide exchange factor SRM1 × 2 (P21827) N-lysine methyltransferase SETD8 × 2 (Q9NQR1) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 5.5;277 K;25 mM sodium acetate pH 5.5, 40 mM sodium citrate,1 mM DTT, 6% PEG2000-MME Resolution 4.50 Å R-free 0.397

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 G; PDBConstruct 1–129; UniProt 2–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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 × 12 DNA 4 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain H; UniProt 5–126 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (149-MER) × 2 DNA (149-MER) × 2 Guanine nucleotide exchange factor SRM1 × 2 (P21827) N-lysine methyltransferase SETD8 × 2 (Q9NQR1) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 5.5;277 K;25 mM sodium acetate pH 5.5, 40 mM sodium citrate,1 mM DTT, 6% PEG2000-MME Resolution 4.50 Å R-free 0.397

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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–122; UniProt 5–126

Guanine nucleotide exchange factor SRM1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P21827

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 × 12 DNA 4 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain K; UniProt 2–482 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 2 DNA (149-MER) × 2 N-lysine methyltransferase SETD8 × 2 (Q9NQR1) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 5.5;277 K;25 mM sodium acetate pH 5.5, 40 mM sodium citrate,1 mM DTT, 6% PEG2000-MME Resolution 4.50 Å R-free 0.397

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 RCC1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 3–483; UniProt 2–482

N-lysine methyltransferase SETD8

Homo sapiens

UniProt Q9NQR1

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 × 12 DNA 4 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain M; UniProt 153–352 Mutation:H347F Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 2 DNA (149-MER) × 2 Guanine nucleotide exchange factor SRM1 × 2 (P21827) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 5.5;277 K;25 mM sodium acetate pH 5.5, 40 mM sodium citrate,1 mM DTT, 6% PEG2000-MME Resolution 4.50 Å R-free 0.397

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.

16 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SETD8_HUMAN
Isoform Q9NQR1-2
PDB entities 8
Chains and sequence ranges Author chain M; PDBConstruct 3–202; UniProt 153–352

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 5hq2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5hq2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5hq2
Deposition date deposition_date2016-01-21
Structure title titleStructural model of Set8 histone H4 Lys20 methyltransferase bound to nucleosome core particle
Keywords keywordschromatin enzyme, chromatin complex, epigenetics, histone methyltransferase, Transferase-DNA complex; Transferase/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.44
Radius of gyration Rg (electron density) rg_electron39.09
Forward intensity I(0) i0372662000.00
Molecular weight molecular_weight111680.0 kDa
Excluded volume excluded_volume120520 ų
Envelope volume envelope_volume236910 ų
Hydration-shell volume shell_volume52254 ų
Envelope diameter envelope_diameter121.4
Shell Rg shell_rg43.40
Envelope Rg envelope_rg37.67
Shape Rg shape_rg39.04
Total Rg total_rg39.44
Total atoms total_atoms7738
Residues n_residues1104
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 dmax118.3
Rg (real space) rg_real39.26
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real3.7270e+08
I(0) uncertainty (real space) i0_real_error6.7240e+06
Rg (reciprocal space) rg_reciprocal39.38
I(0) (reciprocal space) i0_reciprocal372700000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.4
Skewness Skewness skewness0.123
Kurtosis Kurtosis kurtosis-0.663
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21290000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.986; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.668

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)