6zej

Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]

Method: X-RAY DIFFRACTION Dmax: 155.4 Å Quality: GOOD

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

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit,Phosphatase and actin regulator

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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 7–304 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 7–304 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 7–304 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
4 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 7–304 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
5 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain L; UniProt 7–304 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
6 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain O; UniProt 7–304 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271

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 83 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 6–303; UniProt 7–304 Author chain D; PDBConstruct 6–303; UniProt 7–304 Author chain F; PDBConstruct 6–303; UniProt 7–304 Author chain I; PDBConstruct 6–303; UniProt 7–304 Author chain L; PDBConstruct 6–303; UniProt 7–304 Author chain O; PDBConstruct 6–303; UniProt 7–304

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit,Phosphatase and actin regulator

Homo sapiens

UniProt Q4VY12

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 90–144 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 90–144 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 90–144 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
4 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 90–144 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
5 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain L; UniProt 90–144 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271
6 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain O; UniProt 90–144 Mutation:N-terminal Vector derived sequence GHMGS MN MANGANESE (II) ION × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.4;293 K;20% PEG 3350, 0.2M Potassium Citrate Resolution 1.78 Å R-free 0.271

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.

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q4VY12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 309–363; UniProt 90–144 Author chain D; PDBConstruct 309–363; UniProt 90–144 Author chain F; PDBConstruct 309–363; UniProt 90–144 Author chain I; PDBConstruct 309–363; UniProt 90–144 Author chain L; PDBConstruct 309–363; UniProt 90–144 Author chain O; PDBConstruct 309–363; UniProt 90–144

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 6zej

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6zej
Deposition date deposition_date2020-06-16
Structure title titleStructure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]
Keywords keywordsPP1, Phosphatase, Phactr, RPEL, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.37
Radius of gyration Rg (electron density) rg_electron46.18
Forward intensity I(0) i0830679000.00
Molecular weight molecular_weight238070.0 kDa
Excluded volume excluded_volume297420 ų
Envelope volume envelope_volume393270 ų
Hydration-shell volume shell_volume72526 ų
Envelope diameter envelope_diameter167.7
Shell Rg shell_rg49.22
Envelope Rg envelope_rg45.62
Shape Rg shape_rg46.18
Total Rg total_rg46.32
Total atoms total_atoms32870
Residues n_residues2094
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 dmax155.4
Rg (real space) rg_real46.41
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real8.3070e+08
I(0) uncertainty (real space) i0_real_error1.4780e+07
Rg (reciprocal space) rg_reciprocal46.37
I(0) (reciprocal space) i0_reciprocal830600000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.4
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77400000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.738

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6zejA01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id6zejD01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id6zejF01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id6zejI01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id6zejL01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id6zejO01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases

8. Citations (1)

9. Files and Curves (10)