3c1b

The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure

Method: X-RAY DIFFRACTION Dmax: 116.8 Å Quality: GOOD

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

Histone H3-like

Xenopus laevis

UniProt P02302

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone 2, H2bf × 2 (Q28D68) Palindromic 146bp Human Alpha satellite DNA × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;292 K;Manganese chloride, Potassium chloride, Potassium cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.20 Å R-free 0.270

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3L_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; 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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3-like × 2 (P02302) Histone H2A type 1 × 2 (P06897) Histone 2, H2bf × 2 (Q28D68) Palindromic 146bp Human Alpha satellite DNA × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;292 K;Manganese chloride, Potassium chloride, Potassium cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.20 Å R-free 0.270

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 type 1

Xenopus laevis

UniProt P06897

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3-like × 2 (P02302) Histone H4 × 2 (P62799) Histone 2, H2bf × 2 (Q28D68) Palindromic 146bp Human Alpha satellite DNA × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;292 K;Manganese chloride, Potassium chloride, Potassium cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.20 Å R-free 0.270

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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_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 2, H2bf

Xenopus (Silurana) tropicalis

UniProt Q28D68

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded Histone H3-like × 2 (P02302) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Palindromic 146bp Human Alpha satellite DNA × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;292 K;Manganese chloride, Potassium chloride, Potassium cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.20 Å R-free 0.270

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q28D68_XENTR
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

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 3c1b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3c1b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3c1b
Deposition date deposition_date2008-01-22
Structure title titleThe effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure
Keywords keywords;Nucleosome, Dimethylated histone, trimethylated histone, methylation, nucleosomal surface, histone modification, nucleosomal array, chromatin, Acetylation, Chromosomal protein, DNA-binding, Nucleosome core, Nucleus, Phosphoprotein, Ubl conjugation, Structural PROTEIN-DNA COMPLEX ;; Structural PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.88
Radius of gyration Rg (electron density) rg_electron37.16
Forward intensity I(0) i0829529000.00
Molecular weight molecular_weight176470.0 kDa
Excluded volume excluded_volume196150 ų
Envelope volume envelope_volume289460 ų
Hydration-shell volume shell_volume63026 ų
Envelope diameter envelope_diameter120.2
Shell Rg shell_rg44.92
Envelope Rg envelope_rg36.66
Shape Rg shape_rg37.00
Total Rg total_rg37.88
Total atoms total_atoms12041
Residues n_residues1053
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 dmax116.8
Rg (real space) rg_real39.61
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real8.2950e+08
I(0) uncertainty (real space) i0_real_error1.2260e+07
Rg (reciprocal space) rg_reciprocal39.78
I(0) (reciprocal space) i0_reciprocal829700000.0000
Solution quality estimate total_estimate0.8414
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.7
Skewness Skewness skewness0.086
Kurtosis Kurtosis kurtosis-0.699
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha69690000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd3c1ba_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1bb_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1bc_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1bd_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1be_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1bf_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1bg_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3c1bh_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones

CATH v4.4 (8 domains)

Domain ID domain_id3c1bA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3c1bH00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)