4mov

1.45 A Resolution Crystal Structure of Protein Phosphatase 1

Method: X-RAY DIFFRACTION Dmax: 88.5 Å Quality: GOOD

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

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Homo sapiens

UniProt P62136

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 7–300 Not recorded MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1 M HEPES, 1.0 M Lithium Chloride, 20% PEG 6000, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.45 Å R-free 0.167
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 7–300 Not recorded MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;0.1 M HEPES, 1.0 M Lithium Chloride, 20% PEG 6000, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.45 Å R-free 0.167

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.

45 other PDB entries and 87 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–299; UniProt 7–300 Author chain B; PDBConstruct 6–299; UniProt 7–300

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 4mov

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4mov
Deposition date deposition_date2013-09-12
Structure title title1.45 A Resolution Crystal Structure of Protein Phosphatase 1
Keywords keywordscatalytic subunit, Serine/threonine phosphatase, nucleus, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.32
Radius of gyration Rg (electron density) rg_electron26.56
Forward intensity I(0) i070333500.00
Molecular weight molecular_weight65975.0 kDa
Excluded volume excluded_volume82566 ų
Envelope volume envelope_volume95332 ų
Hydration-shell volume shell_volume30196 ų
Envelope diameter envelope_diameter92.6
Shell Rg shell_rg33.56
Envelope Rg envelope_rg26.59
Shape Rg shape_rg26.54
Total Rg total_rg27.34
Total atoms total_atoms4623
Residues n_residues584
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 dmax88.5
Rg (real space) rg_real27.36
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real7.0330e+07
I(0) uncertainty (real space) i0_real_error1.1190e+06
Rg (reciprocal space) rg_reciprocal27.35
I(0) (reciprocal space) i0_reciprocal70330000.0000
Solution quality estimate total_estimate0.8918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25330000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4mova_
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
Domain ID domain_idd4movb_
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 (2 domains)

Domain ID domain_id4movA00
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_id4movB00
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

8. Citations (1)

9. Files and Curves (10)