2iae

Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.

Method: X-RAY DIFFRACTION Dmax: 172.3 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

Mus musculus

UniProt Q76MZ3

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 0–588 Fragment:Aalpha 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 7;298 K;0.1M MES, pH 7.0, 50mM NaCl, 1.4M ammonium sulfate, 0.2M LiCl, 2% 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.316
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 0–588 Fragment:Aalpha 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 7;298 K;0.1M MES, pH 7.0, 50mM NaCl, 1.4M ammonium sulfate, 0.2M LiCl, 2% 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.316

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2AAA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–589; UniProt 0–588 Author chain D; PDBConstruct 1–589; UniProt 0–588

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 30–436 Fragment:B56gamma1 subunit, residues 30-436 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (Q76MZ3) 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 7;298 K;0.1M MES, pH 7.0, 50mM NaCl, 1.4M ammonium sulfate, 0.2M LiCl, 2% 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.316
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 30–436 Fragment:B56gamma1 subunit, residues 30-436 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (Q76MZ3) 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 7;298 K;0.1M MES, pH 7.0, 50mM NaCl, 1.4M ammonium sulfate, 0.2M LiCl, 2% 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.316

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 1–407; UniProt 30–436 Author chain E; PDBConstruct 1–407; UniProt 30–436

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 Fragment:Calpha subunit Mutation:D88N Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (Q76MZ3) 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 7;298 K;0.1M MES, pH 7.0, 50mM NaCl, 1.4M ammonium sulfate, 0.2M LiCl, 2% 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.316
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–309 Fragment:Calpha subunit Mutation:D88N Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (Q76MZ3) 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 7;298 K;0.1M MES, pH 7.0, 50mM NaCl, 1.4M ammonium sulfate, 0.2M LiCl, 2% 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.50 Å R-free 0.316

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 2iae

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2iae
Deposition date deposition_date2006-09-07
Structure title titleCrystal structure of a protein phosphatase 2A (PP2A) holoenzyme.
Keywords keywords;Protein phosphorylation, phosphatase, PP2A, B56, tumor suppressor, methylation, HYDROLASE, TOXIN, 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_guinier52.94
Radius of gyration Rg (electron density) rg_electron53.06
Forward intensity I(0) i01104690000.00
Molecular weight molecular_weight283470.0 kDa
Excluded volume excluded_volume357340 ų
Envelope volume envelope_volume501650 ų
Hydration-shell volume shell_volume82035 ų
Envelope diameter envelope_diameter185.9
Shell Rg shell_rg52.63
Envelope Rg envelope_rg52.20
Shape Rg shape_rg53.06
Total Rg total_rg53.05
Total atoms total_atoms19955
Residues n_residues2519
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 dmax172.3
Rg (real space) rg_real53.17
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real1.1050e+09
I(0) uncertainty (real space) i0_real_error2.1880e+07
Rg (reciprocal space) rg_reciprocal52.73
I(0) (reciprocal space) i0_reciprocal1104000000.0000
Solution quality estimate total_estimate0.8222
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.4
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha59570000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.092

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id2iaeA01
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_id2iaeB01
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_id2iaeC00
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_id2iaeD01
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_id2iaeE01
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_id2iaeF00
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)