4i5n

Structural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6 dephosphorylation

Method: X-RAY DIFFRACTION Dmax: 195.6 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 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 9–589 Fragment:PP2A A alpha subunit (9-589) Non-standard monomer:Yes (specific site not provided by mmCIF) ;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct ; × 1 (Q9Y5P8,Q99741) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha × 1 (P67775) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250
2 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 9–589 Fragment:PP2A A alpha subunit (9-589) Non-standard monomer:Yes (specific site not provided by mmCIF) ;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct ; × 1 (Q9Y5P8,Q99741) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha × 1 (P67775) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250

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 43 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 4–584; UniProt 9–589 Author chain D; PDBConstruct 4–584; UniProt 9–589

;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct ;

Homo sapiens

UniProt Q99741

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 70–90 Fragment:UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha × 1 (P67775) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250
2 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 70–90 Fragment:UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha × 1 (P67775) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 393–413; UniProt 70–90 Author chain E; PDBConstruct 393–413; UniProt 70–90

;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct ;

Homo sapiens

UniProt Q9Y5P8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 122–490 Fragment:UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha × 1 (P67775) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250
2 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 122–490 Fragment:UNP Q9Y5P8 residues 122-490 and UNP Q99741 residues 70-90 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha × 1 (P67775) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250

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.

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

View Construct and Data Evidence
UniProt name P2R3B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–371; UniProt 122–490 Author chain E; PDBConstruct 3–371; UniProt 122–490

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha

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 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) 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) ;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct ; × 1 (Q9Y5P8,Q99741) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250
2 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) 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) ;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta - Cell division control protein 6 homolog chimeric construct ; × 1 (Q9Y5P8,Q99741) Microcystin-LR (MCLR) bound form × 1 CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.75;296 K;0.03M Succinic acid with 7% PEG 3350. Protein (6.2mg/mL) in 10mM tris pH 8.0, 150mM NaCl, 5mM DTT, 1mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 2.80 Å R-free 0.250

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 3–311; UniProt 1–309 Author chain F; 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 4i5n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4i5n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4i5n
Deposition date deposition_date2012-11-28
Structure title titleStructural mechanism of trimeric PP2A holoenzyme involving PR70: insight for Cdc6 dephosphorylation
Keywords keywordsEF Hand, Phosphatase, CDC6 (Substrate), TRANSFERASE-TOXIN complex, HYDROLASE-TOXIN complex; HYDROLASE/TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.89
Radius of gyration Rg (electron density) rg_electron59.76
Forward intensity I(0) i01154970000.00
Molecular weight molecular_weight283480.0 kDa
Excluded volume excluded_volume353810 ų
Envelope volume envelope_volume524950 ų
Hydration-shell volume shell_volume78196 ų
Envelope diameter envelope_diameter218.0
Shell Rg shell_rg54.08
Envelope Rg envelope_rg59.40
Shape Rg shape_rg59.79
Total Rg total_rg59.47
Total atoms total_atoms19753
Residues n_residues2421
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 dmax195.6
Rg (real space) rg_real59.67
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real1.1550e+09
I(0) uncertainty (real space) i0_real_error2.2640e+07
Rg (reciprocal space) rg_reciprocal58.20
I(0) (reciprocal space) i0_reciprocal1152000000.0000
Solution quality estimate total_estimate0.7831
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.7
Skewness Skewness skewness0.619
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha57990000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.759; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.838; Smooth: 0.063

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd4i5na1
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_idd4i5na2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i5nc_
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_idd4i5nd1
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_idd4i5nd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i5nf_
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 (10 domains)

Domain ID domain_id4i5nA00
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_id4i5nB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily230
Domain ID domain_id4i5nB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily220
Domain ID domain_id4i5nB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id4i5nC00
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_id4i5nD00
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_id4i5nE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily230
Domain ID domain_id4i5nE02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily220
Domain ID domain_id4i5nE03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id4i5nF00
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)