2n19

STIL binding to the Polo-box domain 3 of PLK4 regulates centriole duplication

Method: SOLUTION NMR Dmax: 38.8 Å Quality: REASONABLE

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

Serine/threonine-protein kinase PLK4

Homo sapiens

UniProt O00444

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 884–970 Fragment:UNP residues 884-970 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;293.15 K;Ionic strength (raw mmCIF value) 0.03;Pressure ambient NMR sample composition:0.6-1.2 M [U-13C; U-15N; U-2H] PLK4-PB3, 20 mM MOPS, 30 mM sodium chloride, 2 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.6-1.2 M [U-2H,15N,methyl13C/rest-12C-ILV]-PB3 PLK4-PB3, 20 mM MOPS, 30 mM sodium chloride, 2 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1200 mM [U-2H,15N,13C,methyl13C/1H-ILV]-PB3 PLK4-PB3, 20 mM MOPS, 30 mM sodium chloride, 2 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:600 mM [U-2H, U-15N] PLK4-PB3, 20 mM MOPS, 30 mM sodium chloride, 2 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

18 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLK4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–88; UniProt 884–970

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 2n19

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n19
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2n19
Deposition date deposition_date2015-03-24
Structure title titleSTIL binding to the Polo-box domain 3 of PLK4 regulates centriole duplication
Keywords keywordsTRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.63
Radius of gyration Rg (electron density) rg_electron14.29
Forward intensity I(0) i0496206000.00
Molecular weight molecular_weight191840.0 kDa
Excluded volume excluded_volume241580 ų
Envelope volume envelope_volume37253 ų
Hydration-shell volume shell_volume17276 ų
Envelope diameter envelope_diameter62.6
Shell Rg shell_rg24.84
Envelope Rg envelope_rg19.54
Shape Rg shape_rg14.32
Total Rg total_rg14.45
Total atoms total_atoms26960
Residues n_residues1760
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 dmax38.8
Rg (real space) rg_real13.78
Rg uncertainty (real space) rg_real_error0.05
I(0) (real space) i0_real4.7300e+08
I(0) uncertainty (real space) i0_real_error4.2360e+06
Rg (reciprocal space) rg_reciprocal14.71
I(0) (reciprocal space) i0_reciprocal496200000.0000
Solution quality estimate total_estimate0.6769
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.7250
Highest regularization parameter α highest_alpha138700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.957; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2n19a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.223 — Polo-box domain
Superfamily Superfamily superfamilyd.223.1 — Polo-box domain
Family Family familyd.223.1.1 — Swapped Polo-box domain
Domain ID domain_idd2n19a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2n19A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1120 — Arylsulfatase, C-terminal domain
Homologous superfamily homologous superfamily30 — POLO box domain

8. Citations (1)

9. Files and Curves (10)