5w0w

Crystal structure of Protein Phosphatase 2A bound to TIPRL

Method: X-RAY DIFFRACTION Dmax: 206.6 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 9–589 Non-standard monomer:Yes (specific site not provided by mmCIF) TIP41-like protein × 1 (Q8BH58) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 9–589 Non-standard monomer:Yes (specific site not provided by mmCIF) TIP41-like protein × 1 (Q8BH58) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 9–589 Non-standard monomer:Yes (specific site not provided by mmCIF) TIP41-like protein × 1 (Q8BH58) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 9–589 Non-standard monomer:Yes (specific site not provided by mmCIF) TIP41-like protein × 1 (Q8BH58) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246

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 41 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 5–585; UniProt 9–589 Author chain D; PDBConstruct 5–585; UniProt 9–589 Author chain G; PDBConstruct 5–585; UniProt 9–589 Author chain J; PDBConstruct 5–585; UniProt 9–589

TIP41-like protein

Mus musculus

UniProt Q8BH58

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 12–259 Not recorded 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) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 12–259 Not recorded 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) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 12–259 Not recorded 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) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 12–259 Not recorded 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) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIPRL_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–251; UniProt 12–259 Author chain E; PDBConstruct 4–251; UniProt 12–259 Author chain H; PDBConstruct 4–251; UniProt 12–259 Author chain K; PDBConstruct 4–251; UniProt 12–259

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 65 kDa regulatory subunit A alpha isoform × 1 (P30153) TIP41-like protein × 1 (Q8BH58) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) 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) TIP41-like protein × 1 (Q8BH58) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) TIP41-like protein × 1 (Q8BH58) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) TIP41-like protein × 1 (Q8BH58) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;292 K;0.1M citric acid pH 5.2, 9% PEG4000, 0.2M sodium acetate Resolution 3.80 Å R-free 0.246

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 58 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 Author chain F; PDBConstruct 3–311; UniProt 1–309 Author chain I; PDBConstruct 3–311; UniProt 1–309 Author chain L; 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 5w0w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5w0w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5w0w
Deposition date deposition_date2017-06-01
Structure title titleCrystal structure of Protein Phosphatase 2A bound to TIPRL
Keywords keywordscomplex phosphotase phosphotase regulator, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier63.05
Radius of gyration Rg (electron density) rg_electron62.56
Forward intensity I(0) i03432040000.00
Molecular weight molecular_weight496990.0 kDa
Excluded volume excluded_volume622330 ų
Envelope volume envelope_volume965730 ų
Hydration-shell volume shell_volume128030 ų
Envelope diameter envelope_diameter197.8
Shell Rg shell_rg64.86
Envelope Rg envelope_rg60.18
Shape Rg shape_rg62.50
Total Rg total_rg62.83
Total atoms total_atoms34722
Residues n_residues4319
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 dmax206.6
Rg (real space) rg_real62.72
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real3.4320e+09
I(0) uncertainty (real space) i0_real_error6.5190e+07
Rg (reciprocal space) rg_reciprocal63.29
I(0) (reciprocal space) i0_reciprocal3435000000.0000
Solution quality estimate total_estimate0.8838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary74.4
Skewness Skewness skewness0.101
Kurtosis Kurtosis kurtosis-0.594
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha148900000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.828

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5w0wA00
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_id5w0wC00
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_id5w0wD00
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_id5w0wF00
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_id5w0wG00
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_id5w0wI00
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_id5w0wJ00
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_id5w0wL00
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)