8sw6

Protein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide (PhosTAP) version 3

Method: X-RAY DIFFRACTION Dmax: 94.2 Å Quality: REASONABLE

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

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Homo sapiens

UniProt P62136

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 7–300 Fragment:UNP RESIDUES 7-300 PP1-specific Phosphatase-Targeting Peptide version 3 × 1 MN MANGANESE (II) ION × 2 SO4 SULFATE ION × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;289 K;0.1 M HEPES, pH 7.0, 0.1 M lithium sulfate, 30% w/v polyvinylpyrrolidone Resolution 1.76 Å R-free 0.208
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 7–300 Fragment:UNP RESIDUES 7-300 PP1-specific Phosphatase-Targeting Peptide version 3 × 1 MN MANGANESE (II) ION × 2 SO4 SULFATE ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;289 K;0.1 M HEPES, pH 7.0, 0.1 M lithium sulfate, 30% w/v polyvinylpyrrolidone Resolution 1.76 Å R-free 0.208

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.

45 other PDB entries and 87 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–299; UniProt 7–300 Author chain B; PDBConstruct 6–299; UniProt 7–300

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 8sw6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sw6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8sw6
Deposition date deposition_date2023-05-17
Structure title titleProtein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide (PhosTAP) version 3
Keywords keywordsPhosphatase-targeting peptide, complex, phosphatase regulator, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.12
Radius of gyration Rg (electron density) rg_electron27.63
Forward intensity I(0) i085529300.00
Molecular weight molecular_weight73242.0 kDa
Excluded volume excluded_volume91707 ų
Envelope volume envelope_volume107530 ų
Hydration-shell volume shell_volume32130 ų
Envelope diameter envelope_diameter98.0
Shell Rg shell_rg35.09
Envelope Rg envelope_rg27.72
Shape Rg shape_rg27.65
Total Rg total_rg28.30
Total atoms total_atoms5136
Residues n_residues637
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 dmax94.2
Rg (real space) rg_real28.15
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real8.5530e+07
I(0) uncertainty (real space) i0_real_error1.3520e+06
Rg (reciprocal space) rg_reciprocal28.15
I(0) (reciprocal space) i0_reciprocal85530000.0000
Solution quality estimate total_estimate0.5964
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.370
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38870000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 0.109; Positv: 1.000; Valcen: 0.954; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)