2ixm

Structure of human PTPA

Method: X-RAY DIFFRACTION Dmax: 60.2 Å Quality: EXCELLENT

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

;SERINE/THREONINE-PROTEIN PHOSPHATASE 2A REGULATORY SUBUNIT B' ;

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 20–322 Fragment:RESIDUES 20-322 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;PTPA CRYSTALS WERE GROWN USING THE HANGING DROP METHOD AT 20C. 1UL OF PROTEIN (20 MG/ML) WAS MIXED WITH 1 UL OF PRECIPITANT (23% TO 28% PEG 4000, 0.2 M LITHIUM SULFATE, 0.1 M TRIS PH 7.0-8.5 AND 5 MM DTT) WERE EQUILIBRATED AGAINST 0.5 ML OF PRECIPITANT. LARGE PLATE CRYSTALS APPEARED IN 2 TO 3 DAYS. FOR CRYOPROTECTION 5% MPD WAS ADDED TO THE PRECIPITANT SOLUTION. Resolution 1.50 Å R-free 0.221

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 14 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 1–303; UniProt 20–322

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 2ixm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ixm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2ixm
Deposition date deposition_date2006-07-09
Structure title titleStructure of human PTPA
Keywords keywordsPROTEIN PHOSPHATASE 2A, 2 PTPA, PPIASE, HYDROLASE ACTIVATOR; HYDROLASE ACTIVATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.08
Radius of gyration Rg (electron density) rg_electron18.79
Forward intensity I(0) i018648100.00
Molecular weight molecular_weight34393.0 kDa
Excluded volume excluded_volume43706 ų
Envelope volume envelope_volume49362 ų
Hydration-shell volume shell_volume21423 ų
Envelope diameter envelope_diameter63.8
Shell Rg shell_rg25.70
Envelope Rg envelope_rg19.10
Shape Rg shape_rg18.79
Total Rg total_rg19.79
Total atoms total_atoms2431
Residues n_residues300
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 dmax60.2
Rg (real space) rg_real19.93
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.8650e+07
I(0) uncertainty (real space) i0_real_error2.0890e+05
Rg (reciprocal space) rg_reciprocal19.96
I(0) (reciprocal space) i0_reciprocal18650000.0000
Solution quality estimate total_estimate0.9067
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.064
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4411000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2ixma1
Class classa — All alpha proteins
Fold Fold folda.268 — PTPA-like
Superfamily Superfamily superfamilya.268.1 — PTPA-like
Family Family familya.268.1.1 — PTPA-like

CATH v4.4 (1 domains)

Domain ID domain_id2ixmA02
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)