3dw8

Structure of a Protein Phosphatase 2A Holoenzyme with B55 subunit

Method: X-RAY DIFFRACTION Dmax: 175.1 Å Quality: GOOD

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

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Homo sapiens

UniProt P30153

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 A; UniProt 9–589 Fragment:A delta 8: Residues 9-589 Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) 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 5.5;290 K;7-10% PEG 35000, 0.10-0.15 M Sodium citrate pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.85 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 9–589 Fragment:A delta 8: Residues 9-589 Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) 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 5.5;290 K;7-10% PEG 35000, 0.10-0.15 M Sodium citrate pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.85 Å R-free 0.285

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.

34 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2AAA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–582; UniProt 9–589 Author chain D; PDBConstruct 2–582; UniProt 9–589

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform

Homo sapiens

UniProt P63151

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 B; UniProt 1–447 Mutation:I310V Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) 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 5.5;290 K;7-10% PEG 35000, 0.10-0.15 M Sodium citrate pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.85 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–447 Mutation:I310V Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) 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 5.5;290 K;7-10% PEG 35000, 0.10-0.15 M Sodium citrate pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.85 Å R-free 0.285

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.

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

View Construct and Data Evidence
UniProt name 2ABA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–447; UniProt 1–447 Author chain E; PDBConstruct 1–447; UniProt 1–447

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 C; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;290 K;7-10% PEG 35000, 0.10-0.15 M Sodium citrate pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.85 Å R-free 0.285
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) microcystin LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;290 K;7-10% PEG 35000, 0.10-0.15 M Sodium citrate pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.85 Å R-free 0.285

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 3dw8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3dw8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3dw8
Deposition date deposition_date2008-07-21
Structure title titleStructure of a Protein Phosphatase 2A Holoenzyme with B55 subunit
Keywords keywords;holoenzyme, B55, PR55, WD repeat, Hydrolase, Iron, Manganese, Metal-binding, Methylation, Phosphoprotein, Protein phosphatase, 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_guinier53.87
Radius of gyration Rg (electron density) rg_electron53.49
Forward intensity I(0) i01244360000.00
Molecular weight molecular_weight294950.0 kDa
Excluded volume excluded_volume369240 ų
Envelope volume envelope_volume549120 ų
Hydration-shell volume shell_volume86363 ų
Envelope diameter envelope_diameter173.5
Shell Rg shell_rg56.40
Envelope Rg envelope_rg51.17
Shape Rg shape_rg53.49
Total Rg total_rg53.56
Total atoms total_atoms20717
Residues n_residues2586
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 dmax175.1
Rg (real space) rg_real53.76
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real1.2440e+09
I(0) uncertainty (real space) i0_real_error2.4880e+07
Rg (reciprocal space) rg_reciprocal53.94
I(0) (reciprocal space) i0_reciprocal1245000000.0000
Solution quality estimate total_estimate0.8890
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.4
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.594
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36990000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd3dw8a2
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_idd3dw8a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3dw8c_
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_idd3dw8d2
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_idd3dw8d3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3dw8f_
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 (4 domains)

Domain ID domain_id3dw8A00
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_id3dw8C00
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_id3dw8D00
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_id3dw8F00
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)