Function and Biology Details
Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
- Actin family
- Metallo-dependent phosphatase-like
- Actin, conserved site
- ATPase, nucleotide binding domain
- Protein phosphatase 1, regulatory subunit 15A/B, C-terminal
- Calcineurin-like phosphoesterase domain, ApaH type
- Serine-threonine protein phosphatase, N-terminal
1 more domain
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-158948 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Actin, alpha skeletal muscle
Molecule details ›
Chains: A, B, C, L, M
Length: 375 amino acids
Theoretical weight: 41.86 KDa
Source organism: Oryctolagus cuniculus
UniProt:
Sequence domains: Actin
Length: 375 amino acids
Theoretical weight: 41.86 KDa
Source organism: Oryctolagus cuniculus
UniProt:
- Canonical:
P68135 (Residues: 3-377; Coverage: 100%)
Sequence domains: Actin
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Molecule details ›
Chains: D, F, H, J, N
Length: 323 amino acids
Theoretical weight: 37.03 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Length: 323 amino acids
Theoretical weight: 37.03 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P63087 (Residues: 1-323; Coverage: 100%)
Sequence domains:
Protein phosphatase 1 regulatory subunit 15B
Molecule details ›
Chains: E, G, I, K, O
Length: 84 amino acids
Theoretical weight: 10.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Length: 84 amino acids
Theoretical weight: 10.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q5SWA1 (Residues: 631-701; Coverage: 10%)
