› 6zeh

X-ray diffraction
1.3Å resolution

Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha II (1025-1039)] bound to Phactr1 (516-580)

Released:
DOI: 10.2210/pdb6zeh/pdb
PDB entry 6zeh coloured by chain, front view.
PDB entry 6zeh coloured by chain, side view.
PDB entry 6zeh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme.
Fedoryshchak RO, Přechová M, Butler AM, Lee R, O'Reilly N, Flynn HR, Snijders AP, Eder N, Ultanir S, Mouilleron S, Treisman R
Elife 9 (2020)
PMID: 32975518

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-238751 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit; Spectrin alpha chain, non-erythrocytic 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 37.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62136 (Residues: 7-304; Coverage: 90%)
  • Canonical: Q13813 (Residues: 1025-1039; Coverage: 1%)
Gene names: NEAS, PPP1A, PPP1CA, SPTA2, SPTAN1
Sequence domains:
Phosphatase and actin regulator 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 70 amino acids
Theoretical weight: 8.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9C0D0 (Residues: 516-580; Coverage: 11%)
Gene names: KIAA1733, PHACTR1, RPEL1

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand PO4 2 x PO4
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P21
Unit cell:
a: 48.501Å b: 122.388Å c: 69.343Å
α: 90° β: 92.179° γ: 90°
R-values:
R R work R free
0.138 0.137 0.169
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Regulation of Synaptic Transmission and Plasticity by Protein Phosphatase 1.
Foley et al. (2021)
2 more

1 mention without citation

Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme.
Fedoryshchak et al. (2020)