6t90

OCT4-SOX2-bound nucleosome - SHL-6

Method: ELECTRON MICROSCOPY Dmax: 136.1 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–134 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (146-MER) × 1 DNA (146-MER) × 1 Green fluorescent protein,POU domain, class 5, transcription factor 1 × 1 (P42212,Q01860) Transcription factor SOX-2 × 1 (P48431) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 1, 5
Chains and sequence ranges Author chain A; PDBConstruct 4–139; UniProt 1–136 Author chain E; PDBConstruct 4–137; UniProt 1–134

Histone H4

Homo sapiens

UniProt P62805

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information 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 H3.1 × 1 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 1 (P68431) DNA (146-MER) × 1 DNA (146-MER) × 1 Green fluorescent protein,POU domain, class 5, transcription factor 1 × 1 (P42212,Q01860) Transcription factor SOX-2 × 1 (P48431) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–106; UniProt 1–103 Author chain F; PDBConstruct 4–106; UniProt 1–103

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information 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 H3.1 × 1 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 1 (P68431) DNA (146-MER) × 1 DNA (146-MER) × 1 Green fluorescent protein,POU domain, class 5, transcription factor 1 × 1 (P42212,Q01860) Transcription factor SOX-2 × 1 (P48431) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–133; UniProt 1–130 Author chain G; PDBConstruct 4–133; UniProt 1–130

Histone H2B type 1-J

Homo sapiens

UniProt P06899

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–125 Chain H; UniProt 1–125 Not recorded Histone H3.1 × 1 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H3.1 × 1 (P68431) DNA (146-MER) × 1 DNA (146-MER) × 1 Green fluorescent protein,POU domain, class 5, transcription factor 1 × 1 (P42212,Q01860) Transcription factor SOX-2 × 1 (P48431) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 4–128; UniProt 1–125 Author chain H; PDBConstruct 4–128; UniProt 1–125

Green fluorescent protein,POU domain, class 5, transcription factor 1

Homo sapiens

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 1–238 Not recorded Histone H3.1 × 1 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 1 (P68431) DNA (146-MER) × 1 DNA (146-MER) × 1 Transcription factor SOX-2 × 1 (P48431) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 8
Chains and sequence ranges Author chain K; PDBConstruct 23–261; UniProt 1–238

Green fluorescent protein,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 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 1–360 Not recorded Histone H3.1 × 1 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 1 (P68431) DNA (146-MER) × 1 DNA (146-MER) × 1 Transcription factor SOX-2 × 1 (P48431) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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 8
Chains and sequence ranges Author chain K; PDBConstruct 272–631; UniProt 1–360

Transcription factor SOX-2

Homo sapiens

UniProt P48431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain L; UniProt 37–118 Not recorded Histone H3.1 × 1 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 1 (P68431) DNA (146-MER) × 1 DNA (146-MER) × 1 Green fluorescent protein,POU domain, class 5, transcription factor 1 × 1 (P42212,Q01860) PTD PENTANEDIAL × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

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

View Construct and Data Evidence
UniProt name SOX2_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain L; PDBConstruct 24–105; UniProt 37–118

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 6t90

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6t90
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6t90
Deposition date deposition_date2019-10-25
Structure title titleOCT4-SOX2-bound nucleosome - SHL-6
Keywords keywordsnucleosome, OCT4, SOX2, transcription factor, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.58
Radius of gyration Rg (electron density) rg_electron40.69
Forward intensity I(0) i0906210000.00
Molecular weight molecular_weight190400.0 kDa
Excluded volume excluded_volume214720 ų
Envelope volume envelope_volume333760 ų
Hydration-shell volume shell_volume67720 ų
Envelope diameter envelope_diameter136.5
Shell Rg shell_rg46.86
Envelope Rg envelope_rg40.08
Shape Rg shape_rg40.56
Total Rg total_rg41.23
Total atoms total_atoms13031
Residues n_residues1185
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 dmax136.1
Rg (real space) rg_real42.44
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real9.0620e+08
I(0) uncertainty (real space) i0_real_error1.5840e+07
Rg (reciprocal space) rg_reciprocal42.58
I(0) (reciprocal space) i0_reciprocal906400000.0000
Solution quality estimate total_estimate0.8930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.5
Skewness Skewness skewness0.187
Kurtosis Kurtosis kurtosis-0.519
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53940000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6t90B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6t90C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6t90D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6t90F00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6t90G00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6t90H00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6t90K00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology260 — 434 Repressor (Amino-terminal Domain)
Homologous superfamily homologous superfamily40 — lambda repressor-like DNA-binding domains
Domain ID domain_id6t90L00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology30 — DNA Binding (I), subunit A
Homologous superfamily homologous superfamily10 — High mobility group box domain

8. Citations (1)

9. Files and Curves (10)