9skq

Cryo-EM structure of CAK-CDK1-cyclin B1

Method: ELECTRON MICROSCOPY Dmax: 120.6 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 1–309 Not recorded Cyclin-H × 1 (P51946) Cyclin-dependent kinase 7 × 1 (P50613) Cyclin-dependent kinase 1 × 1 (P06493) G2/mitotic-specific cyclin-B1 × 1 (P14635) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 20–328; UniProt 1–309

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 × 5 PDB declaration: pentameric(5) 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) Cyclin-dependent kinase 1 × 1 (P06493) G2/mitotic-specific cyclin-B1 × 1 (P14635) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain J; UniProt 1–346 Not recorded CDK-activating kinase assembly factor MAT1 × 1 (P51948) Cyclin-H × 1 (P51946) Cyclin-dependent kinase 1 × 1 (P06493) G2/mitotic-specific cyclin-B1 × 1 (P14635) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 46–391; UniProt 1–346

Cyclin-dependent kinase 1

Homo sapiens

UniProt P06493

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–297 Non-standard monomer:Yes (specific site not provided by mmCIF) CDK-activating kinase assembly factor MAT1 × 1 (P51948) Cyclin-H × 1 (P51946) Cyclin-dependent kinase 7 × 1 (P50613) G2/mitotic-specific cyclin-B1 × 1 (P14635) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDK1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 6–302; UniProt 1–297

G2/mitotic-specific cyclin-B1

Homo sapiens

UniProt P14635

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–433 Not recorded CDK-activating kinase assembly factor MAT1 × 1 (P51948) Cyclin-H × 1 (P51946) Cyclin-dependent kinase 7 × 1 (P50613) Cyclin-dependent kinase 1 × 1 (P06493) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCNB1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 6–438; UniProt 1–433

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 9skq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9skq
Deposition date deposition_date2025-09-02
Structure title titleCryo-EM structure of CAK-CDK1-cyclin B1
Keywords keywordsComplex, cell cycle, kinase, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.30
Radius of gyration Rg (electron density) rg_electron35.93
Forward intensity I(0) i0279861000.00
Molecular weight molecular_weight138680.0 kDa
Excluded volume excluded_volume175190 ų
Envelope volume envelope_volume228340 ų
Hydration-shell volume shell_volume53387 ų
Envelope diameter envelope_diameter129.3
Shell Rg shell_rg41.84
Envelope Rg envelope_rg35.62
Shape Rg shape_rg35.90
Total Rg total_rg36.45
Total atoms total_atoms9750
Residues n_residues1200
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 dmax120.6
Rg (real space) rg_real36.35
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real2.7990e+08
I(0) uncertainty (real space) i0_real_error4.4050e+06
Rg (reciprocal space) rg_reciprocal36.32
I(0) (reciprocal space) i0_reciprocal279900000.0000
Solution quality estimate total_estimate0.8602
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.8
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis-0.066
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha103300000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.678

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)