2npp

Structure of the Protein Phosphatase 2A Holoenzyme

Method: X-RAY DIFFRACTION Dmax: 168.2 Å Quality: REASONABLE

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

Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform

Homo sapiens

UniProt Q96DH3

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 D; UniProt 1–589 Fragment:scaffolding subunit Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.5 K;15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K Resolution 3.30 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–589 Fragment:scaffolding subunit Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.5 K;15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K Resolution 3.30 Å R-free 0.299

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 Q96DH3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–589; UniProt 1–589 Author chain D; PDBConstruct 1–589; UniProt 1–589

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Homo sapiens

UniProt Q13362

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 E; UniProt 1–439 Not recorded Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform × 1 (Q96DH3) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.5 K;15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K Resolution 3.30 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–439 Not recorded Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform × 1 (Q96DH3) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.5 K;15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K Resolution 3.30 Å R-free 0.299

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.

20 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2A5G_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–449; UniProt 1–439 Author chain E; PDBConstruct 1–449; UniProt 1–439

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

Homo sapiens

UniProt P67775

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 F; UniProt 1–309 Fragment:catalytic subunit Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform × 1 (Q96DH3) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.5 K;15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K Resolution 3.30 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–309 Fragment:catalytic subunit Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform × 1 (Q96DH3) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.5 K;15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K Resolution 3.30 Å R-free 0.299

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.

49 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP2AA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–309; UniProt 1–309 Author chain F; PDBConstruct 1–309; UniProt 1–309

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 2npp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2npp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2npp
Deposition date deposition_date2006-10-28
Structure title titleStructure of the Protein Phosphatase 2A Holoenzyme
Keywords keywordsHEAT repeat, SIGNALING PROTEIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier50.18
Radius of gyration Rg (electron density) rg_electron50.31
Forward intensity I(0) i01161480000.00
Molecular weight molecular_weight290900.0 kDa
Excluded volume excluded_volume366780 ų
Envelope volume envelope_volume530940 ų
Hydration-shell volume shell_volume86713 ų
Envelope diameter envelope_diameter173.4
Shell Rg shell_rg55.77
Envelope Rg envelope_rg48.86
Shape Rg shape_rg50.29
Total Rg total_rg50.56
Total atoms total_atoms20466
Residues n_residues2560
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 dmax168.2
Rg (real space) rg_real50.13
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real1.1610e+09
I(0) uncertainty (real space) i0_real_error2.2460e+07
Rg (reciprocal space) rg_reciprocal50.21
I(0) (reciprocal space) i0_reciprocal1162000000.0000
Solution quality estimate total_estimate0.6457
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.7
Skewness Skewness skewness0.301
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55150000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 0.029; Positv: 1.000; Valcen: 0.999; Smooth: 0.800

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2nppa1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.2 — HEAT repeat
Domain ID domain_idd2nppb1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.20 — B56-like
Domain ID domain_idd2nppc1
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
Domain ID domain_idd2nppd1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.2 — HEAT repeat
Domain ID domain_idd2nppe1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.20 — B56-like
Domain ID domain_idd2nppf1
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

CATH v4.4 (6 domains)

Domain ID domain_id2nppA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2nppB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2nppC00
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_id2nppD00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2nppE00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2nppF00
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)