› 6b67

X-ray diffraction
2.2Å resolution

Human PP2Calpha (PPM1A) complexed with cyclic peptide c(MpSIpYVA)

Released:
DOI: 10.2210/pdb6b67/pdb
PDB entry 6b67 coloured by chain, front view.
PDB entry 6b67 coloured by chain, side view.
PDB entry 6b67 coloured by chain, top view.
Source organisms:
Primary publication:
A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.
Debnath S, Kosek D, Tagad HD, Durell SR, Appella DH, Acevedo R, Grishaev A, Dyda F, Appella E, Mazur SJ
J Biol Chem 293 7993-8008 (2018)
PMID: 29602904

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153030 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein phosphatase 1A Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 296 amino acids
Theoretical weight: 32.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35813 (Residues: 2-297; Coverage: 78%)
Gene names: PPM1A, PPPM1A
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
cyclic peptide c(MpSIpYVA) Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 7 amino acids
Theoretical weight: 1 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 10 x CA
2 modified residues:
Ligand SEP 3 x SEP
Ligand PTR 3 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 159.03Å b: 89.57Å c: 70.05Å
α: 90° β: 113.86° γ: 90°
R-values:
R R work R free
0.169 0.169 0.229
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Recent advances in synthetic and medicinal chemistry of phosphotyrosine and phosphonate-based phosphotyrosine analogues.
Makukhin et al. (2020)
1 more

4 mentions without citation

A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.
Debnath et al. (2018)
3 more