7u0i

Structure of LIN28b nucleosome bound 2 OCT4

Method: ELECTRON MICROSCOPY Dmax: 129.7 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) DNA (162-MER) × 1 DNA (162-MER) × 1 Maltodextrin-binding protein,POU domain, class 5, transcription factor 1 × 2 (A0A376KDN7,Q01860) Single-chain variable fragment × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.1 × 2 (P68431) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) DNA (162-MER) × 1 DNA (162-MER) × 1 Maltodextrin-binding protein,POU domain, class 5, transcription factor 1 × 2 (A0A376KDN7,Q01860) Single-chain variable fragment × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 2-C

Homo sapiens

UniProt Q16777

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 1–129 Chain G; UniProt 1–129 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 2-E × 2 (Q16778) DNA (162-MER) × 1 DNA (162-MER) × 1 Maltodextrin-binding protein,POU domain, class 5, transcription factor 1 × 2 (A0A376KDN7,Q01860) Single-chain variable fragment × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A2C_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 1–129 Author chain G; PDBConstruct 1–129; UniProt 1–129

Histone H2B type 2-E

Homo sapiens

UniProt Q16778

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) DNA (162-MER) × 1 DNA (162-MER) × 1 Maltodextrin-binding protein,POU domain, class 5, transcription factor 1 × 2 (A0A376KDN7,Q01860) Single-chain variable fragment × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

39 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B2E_HUMAN
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

Maltodextrin-binding protein,POU domain, class 5, transcription factor 1

Homo sapiens

UniProt A0A376KDN7

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 26–392 Chain M; UniProt 26–392 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) DNA (162-MER) × 1 DNA (162-MER) × 1 Single-chain variable fragment × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

19 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A376KDN7_ECOLX
Isoform
PDB entities 7
Chains and sequence ranges Author chain L; PDBConstruct 4–370; UniProt 26–392 Author chain M; PDBConstruct 4–370; UniProt 26–392

Maltodextrin-binding 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 138–292 Chain M; UniProt 138–292 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 2-C × 2 (Q16777) Histone H2B type 2-E × 2 (Q16778) DNA (162-MER) × 1 DNA (162-MER) × 1 Single-chain variable fragment × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 7
Chains and sequence ranges Author chain L; PDBConstruct 390–544; UniProt 138–292 Author chain M; PDBConstruct 390–544; UniProt 138–292

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 7u0i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7u0i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7u0i
Deposition date deposition_date2022-02-18
Structure title titleStructure of LIN28b nucleosome bound 2 OCT4
Keywords keywordsnucleosome, transcription factor, transcription, CHROMATIN BINDING PROTEIN-DNA complex, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.48
Radius of gyration Rg (electron density) rg_electron40.91
Forward intensity I(0) i01376880000.00
Molecular weight molecular_weight245550.0 kDa
Excluded volume excluded_volume282050 ų
Envelope volume envelope_volume415920 ų
Hydration-shell volume shell_volume81093 ų
Envelope diameter envelope_diameter131.9
Shell Rg shell_rg49.12
Envelope Rg envelope_rg40.34
Shape Rg shape_rg40.83
Total Rg total_rg41.44
Total atoms total_atoms18108
Residues n_residues1666
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 dmax129.7
Rg (real space) rg_real42.19
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.3770e+09
I(0) uncertainty (real space) i0_real_error2.1810e+07
Rg (reciprocal space) rg_reciprocal42.48
I(0) (reciprocal space) i0_reciprocal1377000000.0000
Solution quality estimate total_estimate0.8921
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.1
Skewness Skewness skewness0.039
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha81800000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7u0iK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7u0iN01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)