8joq

Plk1 polo-box domain bound to HPV18 L2 residues 209-215 with pThr213

Method: X-RAY DIFFRACTION Dmax: 64.5 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 371–594 Fragment:polo-box domain HPV18 L2 peptide × 1 (P06793) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M malate MES Tris buffer pH 6.5, 25% polyethylene glycol 1500 Resolution 1.80 Å R-free 0.250

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 3–226; UniProt 371–594

HPV18 L2 peptide

OrganismNot specified

UniProt P06793

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 209–215 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;0.1M malate MES Tris buffer pH 6.5, 25% polyethylene glycol 1500 Resolution 1.80 Å R-free 0.250

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name VL2_HPV18
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–7; UniProt 209–215

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 8joq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8joq
Deposition date deposition_date2023-06-08
Structure title titlePlk1 polo-box domain bound to HPV18 L2 residues 209-215 with pThr213
Keywords keywordsPlk1, polo-box domain, PBD, HPV, L2, HPV18, REPLICATION, 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_guinier19.18
Radius of gyration Rg (electron density) rg_electron18.07
Forward intensity I(0) i012078000.00
Molecular weight molecular_weight25970.0 kDa
Excluded volume excluded_volume32559 ų
Envelope volume envelope_volume37354 ų
Hydration-shell volume shell_volume17671 ų
Envelope diameter envelope_diameter68.0
Shell Rg shell_rg23.91
Envelope Rg envelope_rg18.34
Shape Rg shape_rg18.05
Total Rg total_rg19.01
Total atoms total_atoms1825
Residues n_residues224
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 dmax64.5
Rg (real space) rg_real19.16
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.2080e+07
I(0) uncertainty (real space) i0_real_error1.3200e+05
Rg (reciprocal space) rg_reciprocal19.16
I(0) (reciprocal space) i0_reciprocal12080000.0000
Solution quality estimate total_estimate0.7742
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.082
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3069000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.698; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; 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)