8g87

Human Oct4 bound to nucleosome with human nMatn1 sequence (focused refinement of Oct4 bound region)

Method: ELECTRON MICROSCOPY Dmax: 65.0 Å Quality: EXCELLENT

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

POU domain, class 5, transcription factor 1

Homo sapiens

UniProt Q01860

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 Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain X; UniProt 1–360 Not recorded nMatn1 DNA (top strand) × 1 nMatn1 DNA (bottom strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM HEPES pH 7.5, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PO5F1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain X; PDBConstruct 36–395; UniProt 1–360

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 8g87

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g87
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g87
Deposition date deposition_date2023-02-17
Structure title titleHuman Oct4 bound to nucleosome with human nMatn1 sequence (focused refinement of Oct4 bound region)
Keywords keywordsOct4, Nucleosome, Pioneer factor, nMatn1 DNA, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier20.33
Radius of gyration Rg (electron density) rg_electron20.07
Forward intensity I(0) i018327500.00
Molecular weight molecular_weight25903.0 kDa
Excluded volume excluded_volume29612 ų
Envelope volume envelope_volume39686 ų
Hydration-shell volume shell_volume17138 ų
Envelope diameter envelope_diameter65.4
Shell Rg shell_rg25.48
Envelope Rg envelope_rg20.15
Shape Rg shape_rg20.06
Total Rg total_rg20.76
Total atoms total_atoms1777
Residues n_residues166
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 dmax65.0
Rg (real space) rg_real20.32
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.8330e+07
I(0) uncertainty (real space) i0_real_error2.0660e+05
Rg (reciprocal space) rg_reciprocal20.32
I(0) (reciprocal space) i0_reciprocal18330000.0000
Solution quality estimate total_estimate0.9053
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2779000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)