› 2o98

X-ray diffraction
2.7Å resolution

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161080 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3-like protein C Chains: A, B
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 27.43 KDa
Source organism: Nicotiana tabacum
Expression system: Escherichia coli
UniProt:
  • Canonical: P93343 (Residues: 1-242; Coverage: 93%)
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Plasma membrane ATPase 3 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 52 amino acids
Theoretical weight: 6.04 KDa
Source organism: Nicotiana plumbaginifolia
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08436 (Residues: 905-956; Coverage: 5%)
Gene name: PMA3
Structure domains: Helix Hairpins

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand FSC 2 x FSC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I4122
Unit cell:
a: 114.37Å b: 114.37Å c: 236.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.178 0.263
Expression system: Escherichia coli

Quick links

Citations

37 review citations

P-type ATPases.
Palmgren et al. (2011)
36 more

14 mentions without citation

Modulators of 14-3-3 Protein-Protein Interactions.
Stevers et al. (2018)
13 more