3fga

Structural Basis of PP2A and Sgo interaction

Method: X-RAY DIFFRACTION Dmax: 114.8 Å Quality: EXCELLENT

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 2–589 Not recorded Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) Shugoshin-like 1 × 1 (Q5FBB7) MICROCYSTIN-LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7;295 K;0.2 M SCTD, 20% w/v Polyethylene glycol 3,350, pH 7, EVAPORATION, temperature 295K Resolution 2.70 Å R-free 0.277

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 7 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 1–588; UniProt 2–589

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 34–436 Fragment:sequence database residues 34-436 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) Shugoshin-like 1 × 1 (Q5FBB7) MICROCYSTIN-LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7;295 K;0.2 M SCTD, 20% w/v Polyethylene glycol 3,350, pH 7, EVAPORATION, temperature 295K Resolution 2.70 Å R-free 0.277

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 25 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 1–403; UniProt 34–436

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–309 Mutation:D88N 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) Shugoshin-like 1 × 1 (Q5FBB7) MICROCYSTIN-LR × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7;295 K;0.2 M SCTD, 20% w/v Polyethylene glycol 3,350, pH 7, EVAPORATION, temperature 295K Resolution 2.70 Å R-free 0.277

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 1–309; UniProt 1–309

Shugoshin-like 1

Homo sapiens

UniProt Q5FBB7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 51–96 Fragment:sequence database residues 51-96 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) 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:EVAPORATION;pH 7;295 K;0.2 M SCTD, 20% w/v Polyethylene glycol 3,350, pH 7, EVAPORATION, temperature 295K Resolution 2.70 Å R-free 0.277

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SGOL1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–47; UniProt 51–96

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 3fga

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fga
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fga
Deposition date deposition_date2008-12-05
Structure title titleStructural Basis of PP2A and Sgo interaction
Keywords keywords;PP2A, shugoshin, Nucleus, Phosphoprotein, Hydrolase, Iron, Manganese, Metal-binding, Methylation, Protein phosphatase, Cell cycle, Cell division, Centromere, Chromosome partition, Mitosis, 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_guinier37.39
Radius of gyration Rg (electron density) rg_electron36.69
Forward intensity I(0) i0335256000.00
Molecular weight molecular_weight152390.0 kDa
Excluded volume excluded_volume192290 ų
Envelope volume envelope_volume252310 ų
Hydration-shell volume shell_volume55706 ų
Envelope diameter envelope_diameter123.5
Shell Rg shell_rg44.42
Envelope Rg envelope_rg36.08
Shape Rg shape_rg36.67
Total Rg total_rg37.26
Total atoms total_atoms10718
Residues n_residues1338
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 dmax114.8
Rg (real space) rg_real37.13
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.3530e+08
I(0) uncertainty (real space) i0_real_error5.2980e+06
Rg (reciprocal space) rg_reciprocal37.29
I(0) (reciprocal space) i0_reciprocal335300000.0000
Solution quality estimate total_estimate0.9044
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.0
Skewness Skewness skewness0.026
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35980000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3fgaa_
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_idd3fgac_
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 (4 domains)

Domain ID domain_id3fgaA01
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_id3fgaB00
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_id3fgaC00
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_id3fgaD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily730 — Single helix bin

8. Citations (1)

9. Files and Curves (10)