4v0w

The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)

Method: X-RAY DIFFRACTION Dmax: 87.1 Å Quality: EXCELLENT

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

SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT

MUS MUSCULUS

UniProt P63087

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 7–300 Fragment:RESIDUES 7-300 PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15B × 1 (Q5SWA1) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;3 M NACL, 0.1 M HEPES, PH7.5 Resolution 1.55 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 7–300 Fragment:RESIDUES 7-300 PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15B × 1 (Q5SWA1) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;3 M NACL, 0.1 M HEPES, PH7.5 Resolution 1.55 Å R-free 0.203

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.

4 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP1G_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–295; UniProt 7–300 Author chain C; PDBConstruct 2–295; UniProt 7–300

PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15B

HOMO SAPIENS

UniProt Q5SWA1

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 B; UniProt 631–669 Fragment:RESIDUES 631-669 SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT × 1 (P63087) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;3 M NACL, 0.1 M HEPES, PH7.5 Resolution 1.55 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 631–669 Fragment:RESIDUES 631-669 SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT × 1 (P63087) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;3 M NACL, 0.1 M HEPES, PH7.5 Resolution 1.55 Å R-free 0.203

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.

4 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PR15B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–44; UniProt 631–669 Author chain D; PDBConstruct 6–44; UniProt 631–669

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 4v0w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v0w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v0w
Deposition date deposition_date2014-09-18
Structure title titleThe crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669)
Keywords keywordsHYDROLASE-HYDROLASE REGULATOR COMPLEX; HYDROLASE/HYDROLASE REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.67
Radius of gyration Rg (electron density) rg_electron27.08
Forward intensity I(0) i081928500.00
Molecular weight molecular_weight72014.0 kDa
Excluded volume excluded_volume90467 ų
Envelope volume envelope_volume106680 ų
Hydration-shell volume shell_volume32346 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg34.75
Envelope Rg envelope_rg27.18
Shape Rg shape_rg27.08
Total Rg total_rg27.89
Total atoms total_atoms5051
Residues n_residues623
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 dmax87.1
Rg (real space) rg_real27.66
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real8.1930e+07
I(0) uncertainty (real space) i0_real_error1.0410e+06
Rg (reciprocal space) rg_reciprocal27.66
I(0) (reciprocal space) i0_reciprocal81930000.0000
Solution quality estimate total_estimate0.9007
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.0
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.501
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30340000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4v0wa1
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_idd4v0wa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4v0wc1
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_idd4v0wc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4v0wA00
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_id4v0wC00
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)