8s30

Crystal structure of human PLK1 Polo-Box Domain in complex with Mis18

Method: X-RAY DIFFRACTION Dmax: 65.3 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 365–603 Not recorded Protein Mis18-alpha × 1 (Q9NYP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.09 M Halogen mix (NaF, NaBr, NaI), 0.1 M buffer system 2 (Sodium HEPES and MOPS) (pH7.5), 37% precipitant mix MPD_P1K_P3350 (MPD (racemic), PEG 1K, PEG 3350) Resolution 1.94 Å R-free 0.271

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 4–242; UniProt 365–603

Protein Mis18-alpha

OrganismNot specified

UniProt Q9NYP9

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 49–55 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein kinase PLK1 × 1 (P53350) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.09 M Halogen mix (NaF, NaBr, NaI), 0.1 M buffer system 2 (Sodium HEPES and MOPS) (pH7.5), 37% precipitant mix MPD_P1K_P3350 (MPD (racemic), PEG 1K, PEG 3350) Resolution 1.94 Å R-free 0.271

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MS18A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–7; UniProt 49–55

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 8s30

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8s30
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8s30
Deposition date deposition_date2024-02-19
Structure title titleCrystal structure of human PLK1 Polo-Box Domain in complex with Mis18
Keywords keywordsPLK1, Mis18 complex, Centromere, Chromosome missegregation, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.95
Radius of gyration Rg (electron density) rg_electron17.94
Forward intensity I(0) i011054900.00
Molecular weight molecular_weight24901.0 kDa
Excluded volume excluded_volume31248 ų
Envelope volume envelope_volume36163 ų
Hydration-shell volume shell_volume17240 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg23.74
Envelope Rg envelope_rg18.28
Shape Rg shape_rg17.92
Total Rg total_rg18.91
Total atoms total_atoms1748
Residues n_residues214
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 dmax65.3
Rg (real space) rg_real18.94
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.1050e+07
I(0) uncertainty (real space) i0_real_error1.5670e+05
Rg (reciprocal space) rg_reciprocal18.95
I(0) (reciprocal space) i0_reciprocal11050000.0000
Solution quality estimate total_estimate0.7785
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.124
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3029000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.716; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)