3m50

X-ray diffraction
2.6Å resolution

Structure of the 14-3-3/PMA2 complex stabilized by Epibestatin

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + H(+)(Side 1) = ADP + phosphate + H(+)(Side 2)
Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-161083 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3-like protein C Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 27.17 KDa
Source organism: Nicotiana tabacum
Expression system: Escherichia coli
UniProt:
  • Canonical: P93343 (Residues: 1-240; Coverage: 92%)
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Plasma membrane ATPase Chain: P
Molecule details ›
Chain: P
Length: 31 amino acids
Theoretical weight: 3.6 KDa
Source organism: Nicotiana plumbaginifolia
Expression system: Escherichia coli
UniProt:
  • Canonical: Q42932 (Residues: 927-956; Coverage: 3%)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: I4122
Unit cell:
a: 97.62Å b: 97.62Å c: 217.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.259 0.255 0.324
Expression system: Escherichia coli