8p6x

Cryo-EM structure of CAK in complex with inhibitor BS-194

Method: ELECTRON MICROSCOPY Dmax: 89.0 Å Quality: GOOD

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

CDK-activating kinase assembly factor MAT1

Homo sapiens

UniProt P51948

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 220–309 Not recorded Cyclin-H × 1 (P51946) Cyclin-dependent kinase 7 × 1 (P50613) NS9 (2S,3S)-3-{[7-(benzylamino)-3-(1-methylethyl)pyrazolo[1,5-a]pyrimidin-5-yl]amino}butane-1,2,4-triol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.90 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.

66 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAT1_HUMAN
Isoform P51948-1
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 4–93; UniProt 220–309

Cyclin-H

Homo sapiens

UniProt P51946

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1–323 Non-standard monomer:Yes (specific site not provided by mmCIF) CDK-activating kinase assembly factor MAT1 × 1 (P51948) Cyclin-dependent kinase 7 × 1 (P50613) NS9 (2S,3S)-3-{[7-(benzylamino)-3-(1-methylethyl)pyrazolo[1,5-a]pyrimidin-5-yl]amino}butane-1,2,4-triol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.90 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.

46 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCNH_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 2–324; UniProt 1–323

Cyclin-dependent kinase 7

Homo sapiens

UniProt P50613

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 1–346 Not recorded CDK-activating kinase assembly factor MAT1 × 1 (P51948) Cyclin-H × 1 (P51946) NS9 (2S,3S)-3-{[7-(benzylamino)-3-(1-methylethyl)pyrazolo[1,5-a]pyrimidin-5-yl]amino}butane-1,2,4-triol × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.90 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.

53 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDK7_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 4–349; UniProt 1–346

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 8p6x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p6x
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8p6x
Deposition date deposition_date2023-05-30
Structure title titleCryo-EM structure of CAK in complex with inhibitor BS-194
Keywords keywordsKinase, Inhibitor, Transcription, Cell Cycle, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier27.60
Radius of gyration Rg (electron density) rg_electron26.65
Forward intensity I(0) i080546100.00
Molecular weight molecular_weight72591.0 kDa
Excluded volume excluded_volume91845 ų
Envelope volume envelope_volume108270 ų
Hydration-shell volume shell_volume33522 ų
Envelope diameter envelope_diameter93.5
Shell Rg shell_rg34.28
Envelope Rg envelope_rg26.79
Shape Rg shape_rg26.63
Total Rg total_rg27.51
Total atoms total_atoms5112
Residues n_residues631
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 dmax89.0
Rg (real space) rg_real27.52
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real8.0550e+07
I(0) uncertainty (real space) i0_real_error1.3270e+06
Rg (reciprocal space) rg_reciprocal27.55
I(0) (reciprocal space) i0_reciprocal80550000.0000
Solution quality estimate total_estimate0.8977
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.416
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24980000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)