4lac

Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A phosphatase activator (PTPA) complex with ATPgammaS

Method: X-RAY DIFFRACTION Dmax: 103.8 Å Quality: GOOD

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

Serine/threonine-protein phosphatase 2A activator

Homo sapiens

UniProt Q15257

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 19–358 Fragment:unp residues 19-358 PP2A Scaffold Subunit A, Truncated, an internal deletion of PP2A A × 1 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) PEG DI(HYDROXYETHYL)ETHER × 1 MN MANGANESE (II) ION × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;0.1M MES at pH6.5 and 10-12% PEG20,000, 1mM ATPgammaS, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.82 Å R-free 0.242

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 4–308; UniProt 19–358

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A activator × 1 (Q15257) PP2A Scaffold Subunit A, Truncated, an internal deletion of PP2A A × 1 PEG DI(HYDROXYETHYL)ETHER × 1 MN MANGANESE (II) ION × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;0.1M MES at pH6.5 and 10-12% PEG20,000, 1mM ATPgammaS, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.82 Å R-free 0.242

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 3
Chains and sequence ranges Author chain C; PDBConstruct 3–311; 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 4lac

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4lac
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4lac
Deposition date deposition_date2013-06-19
Structure title titleCrystal Structure of Protein Phosphatase 2A (PP2A) and PP2A phosphatase activator (PTPA) complex with ATPgammaS
Keywords keywordsPP2A, PTPA, protein phosphatase, signaling pathway regulation, chaperone, Hydrolase-signaling protein complex; Hydrolase/signaling protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.89
Radius of gyration Rg (electron density) rg_electron30.76
Forward intensity I(0) i0135033000.00
Molecular weight molecular_weight94408.0 kDa
Excluded volume excluded_volume118810 ų
Envelope volume envelope_volume143780 ų
Hydration-shell volume shell_volume39177 ų
Envelope diameter envelope_diameter109.6
Shell Rg shell_rg37.50
Envelope Rg envelope_rg31.12
Shape Rg shape_rg30.75
Total Rg total_rg31.36
Total atoms total_atoms6638
Residues n_residues820
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 dmax103.8
Rg (real space) rg_real30.97
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.3500e+08
I(0) uncertainty (real space) i0_real_error1.9780e+06
Rg (reciprocal space) rg_reciprocal30.94
I(0) (reciprocal space) i0_reciprocal135000000.0000
Solution quality estimate total_estimate0.8682
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.443
Kurtosis Kurtosis kurtosis-0.218
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30260000.0000
Real-space data points n_real_points52
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: 0.949; Smooth: 0.827

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4lacb_
Class classa — All alpha proteins
Fold Fold folda.268 — PTPA-like
Superfamily Superfamily superfamilya.268.1 — PTPA-like
Family Family familya.268.1.1 — PTPA-like
Domain ID domain_idd4lacc_
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 (3 domains)

Domain ID domain_id4lacA00
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_id4lacB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1150 — Phosphotyrosyl phosphate activator, C-terminal lid domain
Domain ID domain_id4lacC00
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)