2pkg

Structure of a complex between the A subunit of protein phosphatase 2A and the small t antigen of SV40

Method: X-RAY DIFFRACTION Dmax: 129.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 10–589 Not recorded Small T antigen × 1 (P03081) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;0.2 M MgCl2, 4.5% PEG10000 (w/v), 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.312
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 10–589 Not recorded Small T antigen × 1 (P03081) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;0.2 M MgCl2, 4.5% PEG10000 (w/v), 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.312

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 1–580; UniProt 10–589 Author chain B; PDBConstruct 1–580; UniProt 10–589

Small T antigen

Simian virus 40

UniProt P03081

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 87–174 Fragment:residues 87-174 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;0.2 M MgCl2, 4.5% PEG10000 (w/v), 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.312
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 87–174 Fragment:residues 87-174 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;0.2 M MgCl2, 4.5% PEG10000 (w/v), 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.312

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name TASM_SV40
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–88; UniProt 87–174 Author chain D; PDBConstruct 1–88; UniProt 87–174

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 2pkg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2pkg
Deposition date deposition_date2007-04-17
Structure title titleStructure of a complex between the A subunit of protein phosphatase 2A and the small t antigen of SV40
Keywords keywordsProtein phosphatase 2A, small t antigen, SV40, regulation, Hydrolase REGULATOR-VIRAL PROTEIN COMPLEX; Hydrolase REGULATOR/VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.47
Radius of gyration Rg (electron density) rg_electron39.00
Forward intensity I(0) i0319511000.00
Molecular weight molecular_weight148100.0 kDa
Excluded volume excluded_volume186750 ų
Envelope volume envelope_volume261500 ų
Hydration-shell volume shell_volume57094 ų
Envelope diameter envelope_diameter133.4
Shell Rg shell_rg44.19
Envelope Rg envelope_rg38.26
Shape Rg shape_rg39.01
Total Rg total_rg39.28
Total atoms total_atoms10358
Residues n_residues1318
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 dmax129.2
Rg (real space) rg_real39.45
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real3.1950e+08
I(0) uncertainty (real space) i0_real_error5.1620e+06
Rg (reciprocal space) rg_reciprocal39.46
I(0) (reciprocal space) i0_reciprocal319500000.0000
Solution quality estimate total_estimate0.8891
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.312
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23620000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.879

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2pkga1
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_idd2pkgb1
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_idd2pkgc1
Class classg — Small proteins
Fold Fold foldg.92 — T-antigen specific domain-like
Superfamily Superfamily superfamilyg.92.1 — T-antigen specific domain-like
Family Family familyg.92.1.1 — T-antigen specific domain-like
Domain ID domain_idd2pkgd1
Class classg — Small proteins
Fold Fold foldg.92 — T-antigen specific domain-like
Superfamily Superfamily superfamilyg.92.1 — T-antigen specific domain-like
Family Family familyg.92.1.1 — T-antigen specific domain-like

CATH v4.4 (2 domains)

Domain ID domain_id2pkgA00
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_id2pkgB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)