7qm2

Crystal structure of the PP1/PTG/beta-cyclodextrin ternary complex

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

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 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 7–300 Fragment:phosphatase domain (residues 7-300) Mutation:First residues GHMGS derive from the expression tag Protein phosphatase 1 regulatory subunit 3C × 1 (Q9UQK1) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277 K;0.1 M sodium acetate, 1 M sodium malonate Resolution 2.69 Å R-free 0.213
2 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 7–300 Fragment:phosphatase domain (residues 7-300) Mutation:First residues GHMGS derive from the expression tag Protein phosphatase 1 regulatory subunit 3C × 1 (Q9UQK1) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277 K;0.1 M sodium acetate, 1 M sodium malonate Resolution 2.69 Å R-free 0.213

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 C; PDBConstruct 6–299; UniProt 7–300

Protein phosphatase 1 regulatory subunit 3C

Homo sapiens

UniProt Q9UQK1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 70–264 Fragment:residues 70-264) Mutation:First residues GPLGS derive from the expression tag Serine/threonine-protein phosphatase PP1-alpha catalytic subunit × 1 (P62136) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277 K;0.1 M sodium acetate, 1 M sodium malonate Resolution 2.69 Å R-free 0.213
2 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 70–264 Fragment:residues 70-264) Mutation:First residues GPLGS derive from the expression tag Serine/threonine-protein phosphatase PP1-alpha catalytic subunit × 1 (P62136) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277 K;0.1 M sodium acetate, 1 M sodium malonate Resolution 2.69 Å R-free 0.213

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPR3C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–200; UniProt 70–264 Author chain D; PDBConstruct 6–200; UniProt 70–264

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 7qm2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qm2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qm2
Deposition date deposition_date2021-12-20
Structure title titleCrystal structure of the PP1/PTG/beta-cyclodextrin ternary complex
Keywords keywordsphosphatase, carbohydrate binding, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.40
Radius of gyration Rg (electron density) rg_electron30.50
Forward intensity I(0) i0169531000.00
Molecular weight molecular_weight105080.0 kDa
Excluded volume excluded_volume131990 ų
Envelope volume envelope_volume167880 ų
Hydration-shell volume shell_volume44377 ų
Envelope diameter envelope_diameter101.8
Shell Rg shell_rg38.97
Envelope Rg envelope_rg30.41
Shape Rg shape_rg30.49
Total Rg total_rg31.24
Total atoms total_atoms7394
Residues n_residues895
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_real31.21
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.6950e+08
I(0) uncertainty (real space) i0_real_error2.4810e+06
Rg (reciprocal space) rg_reciprocal31.29
I(0) (reciprocal space) i0_reciprocal169500000.0000
Solution quality estimate total_estimate0.9061
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.3
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.588
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57160000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7qm2A01
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_id7qm2C01
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)