2nym

Crystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit

Method: X-RAY DIFFRACTION Dmax: 164.2 Å Quality: REASONABLE

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

Protein phosphatase 2

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 A; UniProt 8–589 Non-standard monomer:Yes (specific site not provided by mmCIF) 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 K;10-15% PEG8000, 0.1 M Tris-Cl, 0.2 M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.60 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 8–589 Non-standard monomer:Yes (specific site not provided by mmCIF) 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 K;10-15% PEG8000, 0.1 M Tris-Cl, 0.2 M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.60 Å R-free 0.331

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 1–582; UniProt 8–589 Author chain D; PDBConstruct 1–582; UniProt 8–589

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 B; UniProt 38–425 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein phosphatase 2 × 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 K;10-15% PEG8000, 0.1 M Tris-Cl, 0.2 M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.60 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 38–425 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein phosphatase 2 × 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 K;10-15% PEG8000, 0.1 M Tris-Cl, 0.2 M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.60 Å R-free 0.331

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 1–388; UniProt 38–425 Author chain E; PDBConstruct 1–388; UniProt 38–425

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 2–294 Not recorded Protein phosphatase 2 × 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 K;10-15% PEG8000, 0.1 M Tris-Cl, 0.2 M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.60 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 2–294 Not recorded Protein phosphatase 2 × 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 K;10-15% PEG8000, 0.1 M Tris-Cl, 0.2 M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.60 Å R-free 0.331

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 1–293; UniProt 2–294 Author chain F; PDBConstruct 1–293; UniProt 2–294

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 2nym

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2nym
Deposition date deposition_date2006-11-21
Structure title titleCrystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit
Keywords keywordsHEAT repeat, 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_guinier50.52
Radius of gyration Rg (electron density) rg_electron50.65
Forward intensity I(0) i01180750000.00
Molecular weight molecular_weight289650.0 kDa
Excluded volume excluded_volume363010 ų
Envelope volume envelope_volume534720 ų
Hydration-shell volume shell_volume86992 ų
Envelope diameter envelope_diameter174.7
Shell Rg shell_rg55.57
Envelope Rg envelope_rg49.25
Shape Rg shape_rg50.63
Total Rg total_rg50.91
Total atoms total_atoms20212
Residues n_residues2482
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 dmax164.2
Rg (real space) rg_real51.97
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.1730e+09
I(0) uncertainty (real space) i0_real_error2.0760e+07
Rg (reciprocal space) rg_reciprocal50.55
I(0) (reciprocal space) i0_reciprocal1181000000.0000
Solution quality estimate total_estimate0.6822
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.6
Skewness Skewness skewness0.413
Kurtosis Kurtosis kurtosis-0.144
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha1.3540
Highest regularization parameter α highest_alpha50630000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 0.915; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.478

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_idd2nyma1
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_idd2nymb1
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_idd2nymc1
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_idd2nymd1
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_idd2nyme1
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_idd2nymf1
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_id2nymA00
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_id2nymB00
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_id2nymC00
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_id2nymD00
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_id2nymE00
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_id2nymF00
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)