5bsa

Structure of histone H3/H4 in complex with Spt2

Method: X-RAY DIFFRACTION Dmax: 77.1 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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 27–136 Chain B; UniProt 27–136 Fragment:residues 27-136 Histone H4 × 2 (P62799) Protein SPT2 homolog × 2 (Q68D10) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;0.02 M NaCl, 0.2 M HEPES 7.5, 1.6 M ammonium sulfate Resolution 4.61 Å R-free 0.329

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 1–110; UniProt 27–136 Author chain B; PDBConstruct 1–110; UniProt 27–136

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 2–103 Chain D; UniProt 2–103 Not recorded Histone H3.2 × 2 (P84233) Protein SPT2 homolog × 2 (Q68D10) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;0.02 M NaCl, 0.2 M HEPES 7.5, 1.6 M ammonium sulfate Resolution 4.61 Å R-free 0.329

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 C; PDBConstruct 1–102; UniProt 2–103 Author chain D; PDBConstruct 1–102; UniProt 2–103

Protein SPT2 homolog

Homo sapiens

UniProt Q68D10

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 571–685 Chain F; UniProt 571–685 Fragment:residues 571-685 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;0.02 M NaCl, 0.2 M HEPES 7.5, 1.6 M ammonium sulfate Resolution 4.61 Å R-free 0.329

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 SPT2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–115; UniProt 571–685 Author chain F; PDBConstruct 1–115; UniProt 571–685

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 5bsa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5bsa
Deposition date deposition_date2015-06-01
Structure title titleStructure of histone H3/H4 in complex with Spt2
Keywords keywordschaperone, transcription, TRANSCRIPTION REGULATOR; TRANSCRIPTION REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.10
Radius of gyration Rg (electron density) rg_electron24.03
Forward intensity I(0) i028021700.00
Molecular weight molecular_weight39138.0 kDa
Excluded volume excluded_volume48446 ų
Envelope volume envelope_volume66278 ų
Hydration-shell volume shell_volume23318 ų
Envelope diameter envelope_diameter82.1
Shell Rg shell_rg30.51
Envelope Rg envelope_rg24.14
Shape Rg shape_rg24.00
Total Rg total_rg24.97
Total atoms total_atoms2733
Residues n_residues374
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 dmax77.1
Rg (real space) rg_real25.03
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real2.8020e+07
I(0) uncertainty (real space) i0_real_error4.2900e+05
Rg (reciprocal space) rg_reciprocal25.05
I(0) (reciprocal space) i0_reciprocal28020000.0000
Solution quality estimate total_estimate0.8387
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.142
Kurtosis Kurtosis kurtosis-0.659
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4640000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)