4ny3

Human PTPA in complex with peptide

Method: X-RAY DIFFRACTION Dmax: 96.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Serine/threonine-protein phosphatase 2A activator

Homo sapiens

UniProt Q15257

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 22–323 Fragment:UNP Residues 22-323 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) SO4 SULFATE ION × 5 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;2 M (NH4)2SO4 and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.80 Å R-free 0.185
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 22–323 Fragment:UNP Residues 22-323 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) SO4 SULFATE ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;2 M (NH4)2SO4 and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.80 Å R-free 0.185

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–304; UniProt 22–323 Author chain B; PDBConstruct 3–304; UniProt 22–323

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

OrganismNot specified

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 304–309 Fragment:UNP Residues 304-309 Serine/threonine-protein phosphatase 2A activator × 1 (Q15257) SO4 SULFATE ION × 5 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;2 M (NH4)2SO4 and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.80 Å R-free 0.185
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 304–309 Fragment:UNP Residues 304-309 Serine/threonine-protein phosphatase 2A activator × 1 (Q15257) SO4 SULFATE ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;2 M (NH4)2SO4 and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.80 Å R-free 0.185

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–6; UniProt 304–309 Author chain D; PDBConstruct 1–6; UniProt 304–309

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 4ny3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ny3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ny3
Deposition date deposition_date2013-12-10
Structure title titleHuman PTPA in complex with peptide
Keywords keywords;PTPA, PPP2R4, REGULATORY SUBUNIT B' (PR 53), HYDROLASE ACTIVATOR, PROTEIN PHOSPHATASE 2A (PP2A) ;; HYDROLASE ACTIVATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.66
Radius of gyration Rg (electron density) rg_electron27.92
Forward intensity I(0) i076881100.00
Molecular weight molecular_weight71133.0 kDa
Excluded volume excluded_volume89799 ų
Envelope volume envelope_volume107600 ų
Hydration-shell volume shell_volume32812 ų
Envelope diameter envelope_diameter100.0
Shell Rg shell_rg34.60
Envelope Rg envelope_rg27.98
Shape Rg shape_rg27.93
Total Rg total_rg28.56
Total atoms total_atoms5010
Residues n_residues607
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 dmax96.0
Rg (real space) rg_real28.76
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real7.6880e+07
I(0) uncertainty (real space) i0_real_error1.1240e+06
Rg (reciprocal space) rg_reciprocal28.72
I(0) (reciprocal space) i0_reciprocal76880000.0000
Solution quality estimate total_estimate0.8660
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.507
Kurtosis Kurtosis kurtosis-0.166
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha22470000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4ny3A02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1150 — Phosphotyrosyl phosphate activator, C-terminal lid domain
Domain ID domain_id4ny3B02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1150 — Phosphotyrosyl phosphate activator, C-terminal lid domain

8. Citations (1)

9. Files and Curves (10)