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› 6zeg

X-ray diffraction
1.09Å resolution

Structure of PP1-IRSp53 chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)] bound to Phactr1 (516-580)

Released:
DOI: 10.2210/pdb6zeg/pdb
Model geometry
Fit model/data
PDB entry 6zeg coloured by chain, front view.
PDB entry 6zeg coloured by chain, side view.
PDB entry 6zeg 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
OpenAccess logo Elife 9 (2020)
PMID: 32975518

Function and Biology Details

Reaction catalysed: 
[(1) O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate., (2) O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +phosphate., (1) O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate., (2) O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +phosphate.]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158546 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
BAR/IMD domain-containing adapter protein 2; Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 37.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62136 (Residues: 7-304; Coverage: 90%)
  • Canonical: Q9UQB8 (Residues: 448-464; Coverage: 3%)
Gene names: BAIAP2, PPP1A, PPP1CA
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

4 bound ligands:
Ligand MN 4 x MN
Ligand PO4 2 x PO4
Ligand EDO 3 x EDO
Ligand 16P 1 x 16P
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 48.616Å b: 122.394Å c: 69.097Å
α: 90° β: 92.219° γ: 90°
R-values:
R R work R free
0.121 0.12 0.14
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

2 mentions without citation

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