8bjt

Structure of human PLK1 in complex with 2-Allyl-1-[6-(1-hydroxy-1-methyl-ethyl)-pyridin-2-yl]-6-[4-(4-methyl-piperazin-1-yl)-phenylamino]-1,2-dihydro-pyrazolo[3,4-d]pyrimidin-3-one

Method: X-RAY DIFFRACTION Dmax: 71.4 Å Quality: REASONABLE

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

Serine/threonine-protein kinase PLK1

Homo sapiens

UniProt P53350

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 37–330 Not recorded ACT ACETATE ION × 1 8X7 1-[6-(2-hydroxypropan-2-yl)pyridin-2-yl]-6-{[4-(4-methylpiperazin-1-yl)phenyl]amino}-2-(prop-2-en-1-yl)-1,2-dihydro-3H-pyrazolo[3,4-d]pyrimidin-3-one × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;16% w/v PEG4000, 0.1 M Na citrate pH 6.50, 0.6 M Mg acetate, 0.0003 M Zn acetate Resolution 2.19 Å R-free 0.255

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.

84 other PDB entries and 112 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLK1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–294; UniProt 37–330

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 8bjt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bjt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bjt
Deposition date deposition_date2022-11-06
Structure title titleStructure of human PLK1 in complex with 2-Allyl-1-[6-(1-hydroxy-1-methyl-ethyl)-pyridin-2-yl]-6-[4-(4-methyl-piperazin-1-yl)-phenylamino]-1,2-dihydro-pyrazolo[3,4-d]pyrimidin-3-one
Keywords keywords;PLK1, SELECTIVITY RESIDUES, KINASE, POLO-LIKE KINASE, STRUCTURE BASED DRUG DESIGN, ATP-BINDING, NUCLEOTIDE-BINDING, PHOSPHORYLATION, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.00
Radius of gyration Rg (electron density) rg_electron19.88
Forward intensity I(0) i019178800.00
Molecular weight molecular_weight34187.0 kDa
Excluded volume excluded_volume43325 ų
Envelope volume envelope_volume51366 ų
Hydration-shell volume shell_volume21411 ų
Envelope diameter envelope_diameter70.5
Shell Rg shell_rg26.67
Envelope Rg envelope_rg20.36
Shape Rg shape_rg19.86
Total Rg total_rg20.90
Total atoms total_atoms2407
Residues n_residues292
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 dmax71.4
Rg (real space) rg_real20.93
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.9180e+07
I(0) uncertainty (real space) i0_real_error2.4090e+05
Rg (reciprocal space) rg_reciprocal20.94
I(0) (reciprocal space) i0_reciprocal19180000.0000
Solution quality estimate total_estimate0.6371
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6739000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 0.301; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)