8tq2

Structure of the kinase lobe of human CDK8 kinase module

Method: ELECTRON MICROSCOPY Dmax: 88.5 Å Quality: EXCELLENT

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

Mediator of RNA polymerase II transcription subunit 12

Homo sapiens

UniProt Q93074

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–2177 Not recorded Mediator of RNA polymerase II transcription subunit 13 × 1 (Q9UHV7) Cyclin-dependent kinase 8 × 1 (P49336) Cyclin-C × 1 (P24863) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 MED12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–2177; UniProt 1–2177

Mediator of RNA polymerase II transcription subunit 13

Homo sapiens

UniProt Q9UHV7

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–2174 Not recorded Mediator of RNA polymerase II transcription subunit 12 × 1 (Q93074) Cyclin-dependent kinase 8 × 1 (P49336) Cyclin-C × 1 (P24863) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MED13_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–2174; UniProt 1–2174

Cyclin-dependent kinase 8

Homo sapiens

UniProt P49336

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–464 Not recorded Mediator of RNA polymerase II transcription subunit 12 × 1 (Q93074) Mediator of RNA polymerase II transcription subunit 13 × 1 (Q9UHV7) Cyclin-C × 1 (P24863) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDK8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–464; UniProt 1–464

Cyclin-C

Homo sapiens

UniProt P24863

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–283 Not recorded Mediator of RNA polymerase II transcription subunit 12 × 1 (Q93074) Mediator of RNA polymerase II transcription subunit 13 × 1 (Q9UHV7) Cyclin-dependent kinase 8 × 1 (P49336) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCNC_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–283; UniProt 1–283

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 8tq2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tq2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8tq2
Deposition date deposition_date2023-08-06
Structure title titleStructure of the kinase lobe of human CDK8 kinase module
Keywords keywordsTranscription, Mediator, CDK8, MED12, CKM.; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.83
Radius of gyration Rg (electron density) rg_electron27.85
Forward intensity I(0) i091538200.00
Molecular weight molecular_weight78054.0 kDa
Excluded volume excluded_volume99028 ų
Envelope volume envelope_volume125450 ų
Hydration-shell volume shell_volume37098 ų
Envelope diameter envelope_diameter95.0
Shell Rg shell_rg35.73
Envelope Rg envelope_rg27.83
Shape Rg shape_rg27.82
Total Rg total_rg28.78
Total atoms total_atoms5498
Residues n_residues672
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 dmax88.5
Rg (real space) rg_real28.76
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real9.1540e+07
I(0) uncertainty (real space) i0_real_error1.3080e+06
Rg (reciprocal space) rg_reciprocal28.79
I(0) (reciprocal space) i0_reciprocal91540000.0000
Solution quality estimate total_estimate0.9060
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36080000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)