6zk6

Protein Phosphatase 1 (PP1) T320E mutant

Method: X-RAY DIFFRACTION Dmax: 58.0 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–330 Mutation:T320E Non-standard monomer:Yes (specific site not provided by mmCIF) MN MANGANESE (II) ION × 2 FE FE (III) ION × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;PEG 3350, TRIS , lithium chloride Resolution 1.90 Å R-free 0.194

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 88 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 2–331; UniProt 1–330

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 6zk6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6zk6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6zk6
Deposition date deposition_date2020-06-29
Structure title titleProtein Phosphatase 1 (PP1) T320E mutant
Keywords keywordsprotein phosphatase 1 regulation, phosphorylation, phosphomimetic mutant, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.87
Radius of gyration Rg (electron density) rg_electron17.76
Forward intensity I(0) i018838500.00
Molecular weight molecular_weight32978.0 kDa
Excluded volume excluded_volume41127 ų
Envelope volume envelope_volume45026 ų
Hydration-shell volume shell_volume20439 ų
Envelope diameter envelope_diameter58.7
Shell Rg shell_rg24.73
Envelope Rg envelope_rg18.14
Shape Rg shape_rg17.79
Total Rg total_rg18.62
Total atoms total_atoms2306
Residues n_residues289
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 dmax58.0
Rg (real space) rg_real18.74
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real1.8840e+07
I(0) uncertainty (real space) i0_real_error2.1280e+05
Rg (reciprocal space) rg_reciprocal18.76
I(0) (reciprocal space) i0_reciprocal18840000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.153
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4418000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6zk6a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamilyd.159.1 — Metallo-dependent phosphatases
Family Family familyd.159.1.3 — Protein serine/threonine phosphatase

8. Citations (1)

9. Files and Curves (10)