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4v0x

The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-684)

Method: X-RAY DIFFRACTION Dmax: 60.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；2.0 M SODIUM MALONATE, PH6.0 Resolution 1.85 Å R-free 0.222

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.

Other PDB Difference from Current Entry 4V0X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain J 1–323（323 aa） Fragment：RESIDUES 1-323
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 1–323（323 aa） Fragment：RESIDUES 1-323
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain N 1–323（323 aa） Fragment：RESIDUES 1-323
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 1–323（323 aa） Fragment：RESIDUES 1-323
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–323（323 aa） Fragment：RESIDUES 1-323
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0V The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-660) Deposited 2014-09-18 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 7–300（294 aa） Fragment：RESIDUES 7-300
Not recorded MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；2.4M SODIUM MALONATE, PH7.0
Resolution 1.61 Å R-free 0.203
4V0V The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-660) Deposited 2014-09-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 7–300（294 aa） Fragment：RESIDUES 7-300
Not recorded MN MANGANESE (II) ION × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；2.4M SODIUM MALONATE, PH7.0
Resolution 1.61 Å R-free 0.203
4V0W The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669) Deposited 2014-09-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 7–300（294 aa） Fragment：RESIDUES 7-300
Not recorded 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
4V0W The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669) Deposited 2014-09-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 7–300（294 aa） Fragment：RESIDUES 7-300
Not recorded 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
9IJJ In situ structure of the central apparatus in mouse sperm axoneme. Deposited 2024-06-23 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 464 PDB declaration: 464-meric
Chain 4a 1–323（323 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 7.70 Å

4 other PDB entries and 10 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

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 631–684 Fragment：RESIDUES 631-684 PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT × 1 （P63087） MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；2.0 M SODIUM MALONATE, PH6.0 Resolution 1.85 Å R-free 0.222

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.

Other PDB Difference from Current Entry 4V0X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 631–701（71 aa） Fragment：RESIDUES 631-701
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 631–701（71 aa） Fragment：RESIDUES 631-701
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 631–701（71 aa） Fragment：RESIDUES 631-701
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 631–701（71 aa） Fragment：RESIDUES 631-701
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0U The crystal structure of ternary PP1G-PPP1R15B and G-actin complex Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 631–701（71 aa） Fragment：RESIDUES 631-701
Not recorded MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.2M CACL2, 0.1 M HEPES, PH7.0, 20% PEG6000
Resolution 7.88 Å R-free 0.400
4V0V The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-660) Deposited 2014-09-18 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 631–660（30 aa） Fragment：RESIDUES 631-660
Not recorded MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；2.4M SODIUM MALONATE, PH7.0
Resolution 1.61 Å R-free 0.203
4V0V The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-660) Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 631–660（30 aa） Fragment：RESIDUES 631-660
Not recorded MN MANGANESE (II) ION × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；2.4M SODIUM MALONATE, PH7.0
Resolution 1.61 Å R-free 0.203
4V0W The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669) Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 631–669（39 aa） Fragment：RESIDUES 631-669
Not recorded 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
4V0W The crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-669) Deposited 2014-09-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 631–669（39 aa） Fragment：RESIDUES 631-669
Not recorded 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
9HVF Native human PPP1R15B-P-eIF2-eIF2B complex Deposited 2024-12-27 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 411–511（101 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å

4 other PDB entries and 10 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 6–59； UniProt 631–684

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 4v0x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v0x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v0x
Deposition date deposition_date2014-09-18
Structure title titleThe crystal structure of mouse PP1G in complex with truncated human PPP1R15B (631-684)
Keywords keywordsHYDROLASE-HYDROLASE REGULATOR COMPLEX; HYDROLASE/HYDROLASE REGULATOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.76 Å
Radius of gyration Rg (electron density) rg_electron18.54 Å
Forward intensity I(0) i022268600.00
Molecular weight molecular_weight36573.0 kDa
Excluded volume excluded_volume45927 ų
Envelope volume envelope_volume51555 ų
Hydration-shell volume shell_volume22243 ų
Envelope diameter envelope_diameter62.4 Å
Shell Rg shell_rg25.85 Å
Envelope Rg envelope_rg18.96 Å
Shape Rg shape_rg18.52 Å
Total Rg total_rg19.56 Å
Total atoms total_atoms5087
Residues n_residues317
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax60.5 Å
Rg (real space) rg_real19.60 Å
Rg uncertainty (real space) rg_real_error0.25 Å
I(0) (real space) i0_real2.2270e+07
I(0) uncertainty (real space) i0_real_error2.5830e+05
Rg (reciprocal space) rg_reciprocal19.63 Å
I(0) (reciprocal space) i0_reciprocal22270000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6 Å
Skewness Skewness skewness0.123
Kurtosis Kurtosis kurtosis-0.432
Angular range angular_range— – 0.4000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6530000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.982
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4v0xa1
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_idd4v0xa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id4v0xA00
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
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8. Citations (1)

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9. Files and Curves (10)