3c5w

Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme

Method: X-RAY DIFFRACTION Dmax: 111.1 Å Quality: GOOD

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

PP2A A subunit

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 9–46 Chain A; UniProt 400–589 Not recorded PP2A C subunit × 1 (P67775) PP2A-specific methylesterase PME-1 × 1 (Q9Y570) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;25% w/v PEG3350, 100 mM ammonium citrate, and 5 mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.80 Å R-free 0.263

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 44 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 5–42; UniProt 9–46 Author chain A; PDBConstruct 43–232; UniProt 400–589

PP2A C subunit

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–309 Not recorded PP2A A subunit × 1 (P30153) PP2A-specific methylesterase PME-1 × 1 (Q9Y570) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;25% w/v PEG3350, 100 mM ammonium citrate, and 5 mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.80 Å R-free 0.263

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 2–310; UniProt 1–309

PP2A-specific methylesterase PME-1

Homo sapiens

UniProt Q9Y570

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 39–238 Chain P; UniProt 284–386 Not recorded PP2A A subunit × 1 (P30153) PP2A C subunit × 1 (P67775) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;290 K;25% w/v PEG3350, 100 mM ammonium citrate, and 5 mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.80 Å R-free 0.263

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPME1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 5–204; UniProt 39–238 Author chain P; PDBConstruct 208–310; UniProt 284–386

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 3c5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3c5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3c5w
Deposition date deposition_date2008-02-01
Structure title titleComplex between PP2A-specific methylesterase PME-1 and PP2A core enzyme
Keywords keywordsmethylesterase, phosphatase, PP2A, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.78
Radius of gyration Rg (electron density) rg_electron32.77
Forward intensity I(0) i0127325000.00
Molecular weight molecular_weight91616.0 kDa
Excluded volume excluded_volume115160 ų
Envelope volume envelope_volume142430 ų
Hydration-shell volume shell_volume37411 ų
Envelope diameter envelope_diameter115.1
Shell Rg shell_rg38.31
Envelope Rg envelope_rg33.18
Shape Rg shape_rg32.74
Total Rg total_rg33.27
Total atoms total_atoms6441
Residues n_residues816
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 dmax111.1
Rg (real space) rg_real33.01
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real1.2730e+08
I(0) uncertainty (real space) i0_real_error2.1110e+06
Rg (reciprocal space) rg_reciprocal32.91
I(0) (reciprocal space) i0_reciprocal127300000.0000
Solution quality estimate total_estimate0.8585
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.482
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34200000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3c5wc_
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 (3 domains)

Domain ID domain_id3c5wA00
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_id3c5wC00
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_id3c5wP00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain

8. Citations (1)

9. Files and Curves (10)