3k7w

Protein phosphatase 2A core complex bound to dinophysistoxin-2

Method: X-RAY DIFFRACTION Dmax: 127.4 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–589 Not recorded Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) SO4 SULFATE ION × 3 XT2 (2R)-2-hydroxy-3-[(2S,5R,6R,8S)-5-hydroxy-8-{(1R,2E)-3-[(2R,4a'R,5R,6'S,8'R,8a'S)-8'-hydroxy-6'-{(1S,3S)-1-hydroxy-3-[( 2S,6R,11S)-11-methyl-1,7-dioxaspiro[5.5]undec-2-yl]butyl}-7'-methylideneoctahydro-3H,3'H-spiro[furan-2,2'-pyrano[3,2-b]p yran]-5-yl]-1-methylprop-2-en-1-yl}-10-methyl-1,7-dioxaspiro[5.5]undec-10-en-2-yl]-2-methylpropanoic acid × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.2 M LITHIUM SULFATE, 1.5 M AMMONIUM SULFATE, 0.1 M TRIS-CL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.96 Å R-free 0.263

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 44 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 1–589; UniProt 1–589

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 × 2 PDB declaration: dimeric(2) 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) SO4 SULFATE ION × 3 XT2 (2R)-2-hydroxy-3-[(2S,5R,6R,8S)-5-hydroxy-8-{(1R,2E)-3-[(2R,4a'R,5R,6'S,8'R,8a'S)-8'-hydroxy-6'-{(1S,3S)-1-hydroxy-3-[( 2S,6R,11S)-11-methyl-1,7-dioxaspiro[5.5]undec-2-yl]butyl}-7'-methylideneoctahydro-3H,3'H-spiro[furan-2,2'-pyrano[3,2-b]p yran]-5-yl]-1-methylprop-2-en-1-yl}-10-methyl-1,7-dioxaspiro[5.5]undec-10-en-2-yl]-2-methylpropanoic acid × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.2 M LITHIUM SULFATE, 1.5 M AMMONIUM SULFATE, 0.1 M TRIS-CL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.96 Å R-free 0.263

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 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP2AA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; 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 3k7w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3k7w
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3k7w
Deposition date deposition_date2009-10-13
Structure title titleProtein phosphatase 2A core complex bound to dinophysistoxin-2
Keywords keywords;PROTEIN-PROTEIN COMPLEX, HEAT REPEAT, SIGNALING PROTEIN, PHOSPHATASE, LIGAND SPECIFICITY, Acetylation, Polymorphism, Centromere, Cytoplasm, Cytoskeleton, Hydrolase, Iron, Manganese, Metal-binding, Methylation, Nucleus, Phosphoprotein, Protein phosphatase, SIGNALING PROTEIN-HYDROLASE complex ;; SIGNALING PROTEIN/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.86
Radius of gyration Rg (electron density) rg_electron39.53
Forward intensity I(0) i0145113000.00
Molecular weight molecular_weight98723.0 kDa
Excluded volume excluded_volume123950 ų
Envelope volume envelope_volume173230 ų
Hydration-shell volume shell_volume37180 ų
Envelope diameter envelope_diameter125.6
Shell Rg shell_rg45.02
Envelope Rg envelope_rg37.85
Shape Rg shape_rg39.56
Total Rg total_rg39.78
Total atoms total_atoms6923
Residues n_residues869
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 dmax127.4
Rg (real space) rg_real39.98
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real1.4510e+08
I(0) uncertainty (real space) i0_real_error2.7840e+06
Rg (reciprocal space) rg_reciprocal39.92
I(0) (reciprocal space) i0_reciprocal145100000.0000
Solution quality estimate total_estimate0.8356
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.855
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12140000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.542

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3k7wa_
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_idd3k7wc_
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 (2 domains)

Domain ID domain_id3k7wA00
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_id3k7wC00
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)