6jjw

Crystal Structure of KIBRA and PTPN14 complex

Method: X-RAY DIFFRACTION Dmax: 60.6 Å Quality: REASONABLE

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

Protein KIBRA

Mus musculus

UniProt Q5SXA9

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 5–132 Not recorded Peptide from Tyrosine-protein phosphatase non-receptor type 14 × 1 (Q15678) CL CHLORIDE ION × 8 FMT FORMIC ACID × 3 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;700mM magnesium formate, 100mM Bis-Tris Propane (pH 7.0) Resolution 2.40 Å R-free 0.242

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KIBRA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–134; UniProt 5–132

Peptide from Tyrosine-protein phosphatase non-receptor type 14

Homo sapiens

UniProt Q15678

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 U; UniProt 428–455 Not recorded Protein KIBRA × 1 (Q5SXA9) CL CHLORIDE ION × 8 FMT FORMIC ACID × 3 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;700mM magnesium formate, 100mM Bis-Tris Propane (pH 7.0) Resolution 2.40 Å R-free 0.242

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTN14_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain U; PDBConstruct 5–32; UniProt 428–455

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 6jjw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6jjw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6jjw
Deposition date deposition_date2019-02-27
Structure title titleCrystal Structure of KIBRA and PTPN14 complex
Keywords keywordsWW tandem, PY tandem, KIBRA, PTPN14, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.78
Radius of gyration Rg (electron density) rg_electron15.77
Forward intensity I(0) i03957820.00
Molecular weight molecular_weight13304.0 kDa
Excluded volume excluded_volume16206 ų
Envelope volume envelope_volume20134 ų
Hydration-shell volume shell_volume11409 ų
Envelope diameter envelope_diameter59.6
Shell Rg shell_rg20.60
Envelope Rg envelope_rg16.16
Shape Rg shape_rg15.69
Total Rg total_rg16.89
Total atoms total_atoms928
Residues n_residues109
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 dmax60.6
Rg (real space) rg_real16.80
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real3.9580e+06
I(0) uncertainty (real space) i0_real_error4.9110e+04
Rg (reciprocal space) rg_reciprocal16.80
I(0) (reciprocal space) i0_reciprocal3958000.0000
Solution quality estimate total_estimate0.6348
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.162
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha802700.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 0.394; Positv: 1.000; Valcen: 0.881; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)