9f6y

CryoEM structure of Human Mediator subunit MED23 complexed with phosphorylated Elk-1 transcription factor

Method: ELECTRON MICROSCOPY Dmax: 136.3 Å Quality: GOOD

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

Mediator of RNA polymerase II transcription subunit 23

Homo sapiens

UniProt Q9ULK4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1368 Not recorded Green fluorescent protein,ETS domain-containing protein Elk-1 × 1 (P42212,P19419) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MED23_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1368; UniProt 1–1368

Green fluorescent protein,ETS domain-containing protein Elk-1

Homo sapiens

UniProt P19419

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 308–401 Non-standard monomer:Yes (specific site not provided by mmCIF) Mediator of RNA polymerase II transcription subunit 23 × 1 (Q9ULK4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELK1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 242–335; UniProt 308–401

Green fluorescent protein,ETS domain-containing protein Elk-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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–238 Non-standard monomer:Yes (specific site not provided by mmCIF) Mediator of RNA polymerase II transcription subunit 23 × 1 (Q9ULK4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–239; UniProt 1–238

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 9f6y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f6y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f6y
Deposition date deposition_date2024-05-02
最后修订 last_revision2025-04-30
Structure title titleCryoEM structure of Human Mediator subunit MED23 complexed with phosphorylated Elk-1 transcription factor
Keywords keywordsMediator complex, transcription factor, Med23, ELK-1, phosphorylation, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.78
Radius of gyration Rg (electron density) rg_electron38.59
Forward intensity I(0) i0280095000.00
Molecular weight molecular_weight142010.0 kDa
Excluded volume excluded_volume180330 ų
Envelope volume envelope_volume240270 ų
Hydration-shell volume shell_volume52873 ų
Envelope diameter envelope_diameter142.2
Shell Rg shell_rg43.30
Envelope Rg envelope_rg38.86
Shape Rg shape_rg38.57
Total Rg total_rg38.97
Total atoms total_atoms10008
Residues n_residues1234
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 dmax136.3
Rg (real space) rg_real38.94
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real2.8010e+08
I(0) uncertainty (real space) i0_real_error5.1730e+06
Rg (reciprocal space) rg_reciprocal38.85
I(0) (reciprocal space) i0_reciprocal280100000.0000
Solution quality estimate total_estimate0.8622
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.9
Skewness Skewness skewness0.432
Kurtosis Kurtosis kurtosis-0.261
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha100300000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)