4ld9

Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle

Method: X-RAY DIFFRACTION Dmax: 136.8 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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence reverse × 1 Widom 601 sequence forward × 1 Regulatory protein SIR3 × 2 (P06701) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293.15 K;50 mM MES pH 6.5, 12% PEG 400, 12 mM MnCl2, 100 mM NaCl, 10 mM EDTA, VAPOR DIFFUSION, temperature 293.15K Resolution 3.31 Å R-free 0.295

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 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence reverse × 1 Widom 601 sequence forward × 1 Regulatory protein SIR3 × 2 (P06701) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293.15 K;50 mM MES pH 6.5, 12% PEG 400, 12 mM MnCl2, 100 mM NaCl, 10 mM EDTA, VAPOR DIFFUSION, temperature 293.15K Resolution 3.31 Å R-free 0.295

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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence reverse × 1 Widom 601 sequence forward × 1 Regulatory protein SIR3 × 2 (P06701) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293.15 K;50 mM MES pH 6.5, 12% PEG 400, 12 mM MnCl2, 100 mM NaCl, 10 mM EDTA, VAPOR DIFFUSION, temperature 293.15K Resolution 3.31 Å R-free 0.295

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 1–130; UniProt 1–130 Author chain G; PDBConstruct 1–130; UniProt 1–130

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Widom 601 sequence reverse × 1 Widom 601 sequence forward × 1 Regulatory protein SIR3 × 2 (P06701) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293.15 K;50 mM MES pH 6.5, 12% PEG 400, 12 mM MnCl2, 100 mM NaCl, 10 mM EDTA, VAPOR DIFFUSION, temperature 293.15K Resolution 3.31 Å R-free 0.295

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 D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126

Regulatory protein SIR3

Saccharomyces cerevisiae

UniProt P06701

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 2–229 Chain L; UniProt 2–229 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence reverse × 1 Widom 601 sequence forward × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293.15 K;50 mM MES pH 6.5, 12% PEG 400, 12 mM MnCl2, 100 mM NaCl, 10 mM EDTA, VAPOR DIFFUSION, temperature 293.15K Resolution 3.31 Å R-free 0.295

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIR3_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 2–229; UniProt 2–229 Author chain L; PDBConstruct 2–229; UniProt 2–229

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 4ld9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ld9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ld9
Deposition date deposition_date2013-06-24
Structure title titleCrystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle
Keywords keywords;BETA BARREL, PROTEIN-DNA COMPLEX, DOUBLE HELIX, alpha-helix, beta-sheet, double stranded DNA, chromatin binding, chromatin, N-terminal acetylation, nucleus, NUCLEAR PROTEIN-TRANSCRIPTION-DNA complex ;; NUCLEAR PROTEIN/TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.77
Radius of gyration Rg (electron density) rg_electron40.24
Forward intensity I(0) i01133210000.00
Molecular weight molecular_weight220010.0 kDa
Excluded volume excluded_volume251580 ų
Envelope volume envelope_volume374620 ų
Hydration-shell volume shell_volume75144 ų
Envelope diameter envelope_diameter144.9
Shell Rg shell_rg47.92
Envelope Rg envelope_rg39.59
Shape Rg shape_rg40.20
Total Rg total_rg40.66
Total atoms total_atoms15140
Residues n_residues1431
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 dmax136.8
Rg (real space) rg_real41.51
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.1330e+09
I(0) uncertainty (real space) i0_real_error1.9370e+07
Rg (reciprocal space) rg_reciprocal41.76
I(0) (reciprocal space) i0_reciprocal1134000000.0000
Solution quality estimate total_estimate0.8803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.6
Skewness Skewness skewness0.062
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118900000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id4ld9A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9E00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9F00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9G00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9H00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ld9K00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily490 — Bromo adjacent homology (BAH) domain
Domain ID domain_id4ld9L00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily490 — Bromo adjacent homology (BAH) domain

8. Citations (1)

9. Files and Curves (10)