4iyp

structure of the nPP2Ac-alpha4 complex

Method: X-RAY DIFFRACTION Dmax: 95.7 Å Quality: GOOD

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

Immunoglobulin-binding protein 1

Homo sapiens

UniProt P78318

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 2–234 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;291 K;12-15% PEG3350 (v/v), 0.3 M Na/K tartrate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.80 Å R-free 0.222

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 IGBP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–222; UniProt 2–234

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 6–153 Non-standard monomer:Yes (specific site not provided by mmCIF) Immunoglobulin-binding protein 1 × 1 (P78318) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;291 K;12-15% PEG3350 (v/v), 0.3 M Na/K tartrate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.80 Å R-free 0.222

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 2
Chains and sequence ranges Author chain C; PDBConstruct 4–151; UniProt 6–153

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 4iyp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4iyp
Deposition date deposition_date2013-01-29
Structure title titlestructure of the nPP2Ac-alpha4 complex
Keywords keywordsalpha4, PP2A, latency, helix motif, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.84
Radius of gyration Rg (electron density) rg_electron22.87
Forward intensity I(0) i025480700.00
Molecular weight molecular_weight38307.0 kDa
Excluded volume excluded_volume47774 ų
Envelope volume envelope_volume62519 ų
Hydration-shell volume shell_volume23429 ų
Envelope diameter envelope_diameter99.9
Shell Rg shell_rg29.07
Envelope Rg envelope_rg23.71
Shape Rg shape_rg22.79
Total Rg total_rg23.90
Total atoms total_atoms2674
Residues n_residues317
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 dmax95.7
Rg (real space) rg_real23.95
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real2.5480e+07
I(0) uncertainty (real space) i0_real_error3.4660e+05
Rg (reciprocal space) rg_reciprocal23.92
I(0) (reciprocal space) i0_reciprocal25480000.0000
Solution quality estimate total_estimate0.7608
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis0.259
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5863000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.419; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.641; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4iypA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily540 — TAP42-like family

8. Citations (1)

9. Files and Curves (10)