7sd0

Cryo-EM structure of the SHOC2:PP1C:MRAS complex

Method: ELECTRON MICROSCOPY Dmax: 91.9 Å Quality: GOOD

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

Leucine-rich repeat protein SHOC-2

Homo sapiens

UniProt Q9UQ13

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 2–582 Not recorded Ras-related protein M-Ras × 1 (O14807) Serine/threonine-protein phosphatase PP1-gamma catalytic subunit × 1 (P36873) GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Used the "perpetually hydrated" method of applying graphene oxide. (Cheung et al., 2018) Resolution 2.95 Å

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.

12 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SHOC2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–582; UniProt 2–582

Ras-related protein M-Ras

Homo sapiens

UniProt O14807

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 B; UniProt 1–208 Not recorded Leucine-rich repeat protein SHOC-2 × 1 (Q9UQ13) Serine/threonine-protein phosphatase PP1-gamma catalytic subunit × 1 (P36873) GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Used the "perpetually hydrated" method of applying graphene oxide. (Cheung et al., 2018) Resolution 2.95 Å

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.

10 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASM_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–210; UniProt 1–208

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Homo sapiens

UniProt P36873

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 1–323 Not recorded Leucine-rich repeat protein SHOC-2 × 1 (Q9UQ13) Ras-related protein M-Ras × 1 (O14807) GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Used the "perpetually hydrated" method of applying graphene oxide. (Cheung et al., 2018) Resolution 2.95 Å

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP1G_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–325; UniProt 1–323

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 7sd0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7sd0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7sd0
Deposition date deposition_date2021-09-29
Structure title titleCryo-EM structure of the SHOC2:PP1C:MRAS complex
Keywords keywordsPhosphatase, leucine rich repeat, RAF, complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.62
Radius of gyration Rg (electron density) rg_electron29.75
Forward intensity I(0) i0186873000.00
Molecular weight molecular_weight110130.0 kDa
Excluded volume excluded_volume138690 ų
Envelope volume envelope_volume172100 ų
Hydration-shell volume shell_volume46659 ų
Envelope diameter envelope_diameter97.1
Shell Rg shell_rg38.24
Envelope Rg envelope_rg29.51
Shape Rg shape_rg29.75
Total Rg total_rg30.53
Total atoms total_atoms7729
Residues n_residues965
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 dmax91.9
Rg (real space) rg_real30.43
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.8690e+08
I(0) uncertainty (real space) i0_real_error2.7530e+06
Rg (reciprocal space) rg_reciprocal30.52
I(0) (reciprocal space) i0_reciprocal186900000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.6
Skewness Skewness skewness0.155
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72450000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7sd0B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7sd0C01
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)