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The cyanobacterial PP2C-like phosphatase tppha requires three metals in the catalytic center for efficient catalysis

Analyse The cyanobacterial PP2C-like phosphatase tppha requires three metals in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y09
Type
protein
Length
236 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein serin-threonin phosphatase
UniProt
Q8DGS1
Ligands
CA, MG
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein serin-threonin phosphataseprotein23634% helix, 28% strandQ8DGS1

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains A
  • MG · Magnesium ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.400.7716empty
2740.340.7616CA

Compared structures

  • 2Y09 · The cyanobacterial PP2C-like phosphatase tPphA requires three metals in the catalytic… · the same entry in another collection · chain A against A, TM-score 1.00

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