5yf4

A kinase complex MST4-MOB4

Method: X-RAY DIFFRACTION Dmax: 52.5 Å Quality: GOOD

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

MOB-like protein phocein

Homo sapiens

UniProt Q9Y3A3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 53–210 Fragment:UNP residues 53-210 Peptide from Serine/threonine-protein kinase 26 × 2 (Q9P289) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1M HEPES, pH 7.5, 30% PEG 1000 Resolution 1.90 Å R-free 0.198

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHOCN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–162; UniProt 53–210

Peptide from Serine/threonine-protein kinase 26

OrganismNot specified

UniProt Q9P289

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 320–335 Non-standard monomer:Yes (specific site not provided by mmCIF) MOB-like protein phocein × 2 (Q9Y3A3) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1M HEPES, pH 7.5, 30% PEG 1000 Resolution 1.90 Å R-free 0.198

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.

8 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STK26_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–16; UniProt 320–335

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 5yf4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5yf4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5yf4
Deposition date deposition_date2017-09-20
Structure title titleA kinase complex MST4-MOB4
Keywords keywordsKinase, Complex, Phosphorylation, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.48
Radius of gyration Rg (electron density) rg_electron14.30
Forward intensity I(0) i05226550.00
Molecular weight molecular_weight15888.0 kDa
Excluded volume excluded_volume19640 ų
Envelope volume envelope_volume22356 ų
Hydration-shell volume shell_volume13121 ų
Envelope diameter envelope_diameter51.1
Shell Rg shell_rg20.35
Envelope Rg envelope_rg14.77
Shape Rg shape_rg14.31
Total Rg total_rg15.45
Total atoms total_atoms1105
Residues n_residues138
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 dmax52.5
Rg (real space) rg_real15.38
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real5.2270e+06
I(0) uncertainty (real space) i0_real_error5.8710e+04
Rg (reciprocal space) rg_reciprocal15.39
I(0) (reciprocal space) i0_reciprocal5227000.0000
Solution quality estimate total_estimate0.8608
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.137
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1013000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.733; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)