8uxq

Structure of Heterochromatin Protein 1 (HP1) alpha in complex with an H2A.Z nucleosome

Method: ELECTRON MICROSCOPY Dmax: 115.8 Å Quality: EXCELLENT

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

Chromobox protein homolog 5

Homo sapiens

UniProt P45973

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: 12-meric(12) Consistent with all polymer counts Chain A; UniProt 2–191 Chain C; UniProt 2–191 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A.Z × 2 (P0C0S6) Histone H2B 1.1 × 2 (P02281) DNA Widom601 (208bp) strand1 × 1 DNA Widom601 (208bp) strand2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 Å

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.

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

View Construct and Data Evidence
UniProt name CBX5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–195; UniProt 2–191 Author chain C; PDBConstruct 6–195; UniProt 2–191

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: 12-meric(12) Consistent with all polymer counts Chain E; UniProt 2–136 Chain K; UniProt 2–136 Mutation:C110A Chromobox protein homolog 5 × 2 (P45973) Histone H4 × 2 (P62799) Histone H2A.Z × 2 (P0C0S6) Histone H2B 1.1 × 2 (P02281) DNA Widom601 (208bp) strand1 × 1 DNA Widom601 (208bp) strand2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 Å

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 2
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 2–136 Author chain K; 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 × 10 DNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain F; UniProt 2–103 Chain L; UniProt 2–103 Not recorded Chromobox protein homolog 5 × 2 (P45973) Histone H3.2 × 2 (P84233) Histone H2A.Z × 2 (P0C0S6) Histone H2B 1.1 × 2 (P02281) DNA Widom601 (208bp) strand1 × 1 DNA Widom601 (208bp) strand2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 Å

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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–102; UniProt 2–103 Author chain L; PDBConstruct 1–102; UniProt 2–103

Histone H2A.Z

Mus musculus

UniProt P0C0S6

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: 12-meric(12) Consistent with all polymer counts Chain G; UniProt 2–128 Chain M; UniProt 2–128 Not recorded Chromobox protein homolog 5 × 2 (P45973) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA Widom601 (208bp) strand1 × 1 DNA Widom601 (208bp) strand2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AZ_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–127; UniProt 2–128 Author chain M; PDBConstruct 1–127; UniProt 2–128

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: 12-meric(12) Consistent with all polymer counts Chain H; UniProt 2–126 Chain N; UniProt 2–126 Not recorded Chromobox protein homolog 5 × 2 (P45973) Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A.Z × 2 (P0C0S6) DNA Widom601 (208bp) strand1 × 1 DNA Widom601 (208bp) strand2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 Å

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 5
Chains and sequence ranges Author chain H; PDBConstruct 1–125; UniProt 2–126 Author chain N; 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 8uxq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uxq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8uxq
Deposition date deposition_date2023-11-09
Structure title titleStructure of Heterochromatin Protein 1 (HP1) alpha in complex with an H2A.Z nucleosome
Keywords keywordsheterochromatin, nucleosome, chromatin, GENE REGULATION, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.55
Radius of gyration Rg (electron density) rg_electron37.31
Forward intensity I(0) i0751702000.00
Molecular weight molecular_weight182750.0 kDa
Excluded volume excluded_volume212030 ų
Envelope volume envelope_volume332380 ų
Hydration-shell volume shell_volume70994 ų
Envelope diameter envelope_diameter121.5
Shell Rg shell_rg45.95
Envelope Rg envelope_rg36.64
Shape Rg shape_rg37.21
Total Rg total_rg38.02
Total atoms total_atoms12603
Residues n_residues1276
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 dmax115.8
Rg (real space) rg_real39.17
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real7.5170e+08
I(0) uncertainty (real space) i0_real_error1.1660e+07
Rg (reciprocal space) rg_reciprocal39.41
I(0) (reciprocal space) i0_reciprocal751900000.0000
Solution quality estimate total_estimate0.9055
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.1
Skewness Skewness skewness0.001
Kurtosis Kurtosis kurtosis-0.615
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64150000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)