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Structure of protein SERINE/THREONINE phosphatase from saccharomyces cerevisiae with similarity to human phosphatase PP5

Analyse Structure of protein SERINE/THREONINE phosphatase from saccharomyces cerevisiae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ICF
Type
protein
Length
631 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SERINE/THREONINE-protein phosphatase T
EC
3.1.3.16
UniProt
P53043
Ligands
FE, NA, PO4, CL
Pockets
2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASERINE/THREONINE-protein phosphatase T (EC 3.1.3.16)protein31634% helix, 20% strandP53043
BSERINE/THREONINE-protein phosphatase T (EC 3.1.3.16)protein31535% helix, 20% strandP53043

Ligands and binding sites

  • FE · Fe (III) ion · metal · 4 copies · chains A, B
  • NA · Sodium ion · metal · chains A, B
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B
  • CL · Chloride ion · ion
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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
11120.410.7513empty
21160.390.7521empty

Interfaces

1 interface between chains.

  • A–B · 820 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 modified (engineered).

Compared structures

  • 3ICF · Structure of Protein serine/threonine phosphatase from Saccharomyces cerevisiae with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P53043 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase T (P53043) · a predicted model of the same protein · chain A against A, TM-score 0.99

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