6p8f

Crystal structure of CDK4 in complex with CyclinD1 and P27

Method: X-RAY DIFFRACTION Dmax: 88.5 Å Quality: EXCELLENT

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

G1/S-specific cyclin-D1

Homo sapiens

UniProt P24385

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 A; UniProt 19–267 Not recorded Cyclin-dependent kinase 4 × 1 (P11802) Cyclin-dependent kinase inhibitor 1B × 1 (P46527) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;100mM Tris (7.0) 17% PEG 3350 100 mM CaCl2 10 mM MgCl2 Resolution 2.89 Å R-free 0.242

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCND1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–249; UniProt 19–267

Cyclin-dependent kinase 4

Homo sapiens

UniProt P11802

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 B; UniProt 2–303 Mutation:G48E, G49E G1/S-specific cyclin-D1 × 1 (P24385) Cyclin-dependent kinase inhibitor 1B × 1 (P46527) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;100mM Tris (7.0) 17% PEG 3350 100 mM CaCl2 10 mM MgCl2 Resolution 2.89 Å R-free 0.242

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.

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

View Construct and Data Evidence
UniProt name CDK4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–302; UniProt 2–303

Cyclin-dependent kinase inhibitor 1B

Homo sapiens

UniProt P46527

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 C; UniProt 25–106 Non-standard monomer:Yes (specific site not provided by mmCIF) G1/S-specific cyclin-D1 × 1 (P24385) Cyclin-dependent kinase 4 × 1 (P11802) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;100mM Tris (7.0) 17% PEG 3350 100 mM CaCl2 10 mM MgCl2 Resolution 2.89 Å R-free 0.242

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.

16 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDN1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–82; UniProt 25–106

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 6p8f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6p8f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6p8f
Deposition date deposition_date2019-06-07
Structure title titleCrystal structure of CDK4 in complex with CyclinD1 and P27
Keywords keywordsCyclin-dependent kinase, kinase inhibitor, CELL CYCLE, transferase; cell cycle, transferase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.31
Radius of gyration Rg (electron density) rg_electron27.25
Forward intensity I(0) i066544300.00
Molecular weight molecular_weight64096.0 kDa
Excluded volume excluded_volume80536 ų
Envelope volume envelope_volume101280 ų
Hydration-shell volume shell_volume30780 ų
Envelope diameter envelope_diameter88.8
Shell Rg shell_rg34.67
Envelope Rg envelope_rg27.19
Shape Rg shape_rg27.27
Total Rg total_rg27.97
Total atoms total_atoms4498
Residues n_residues561
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_real28.21
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real6.6540e+07
I(0) uncertainty (real space) i0_real_error1.0810e+06
Rg (reciprocal space) rg_reciprocal28.24
I(0) (reciprocal space) i0_reciprocal66550000.0000
Solution quality estimate total_estimate0.9096
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.6
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.628
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21110000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6p8fb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id6p8fA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily10 — Cyclin-like
Domain ID domain_id6p8fA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily10 — Cyclin-like
Domain ID domain_id6p8fB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id6p8fB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)