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Crystal structure of the SERINE/THREONINE phosphatase domain of human PPM1B

Analyse Crystal structure of the SERINE/THREONINE phosphatase domain of human PPM1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2P8E
Type
protein
Length
559 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PPM1B beta isoform variant 6
EC
3.1.3.16
UniProt
Q4J6C0
Ligands
MG
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APPM1B beta isoform variant 6 (EC 3.1.3.16)protein27829% helix, 35% strandQ4J6C0
BPPM1B beta isoform variant 6 (EC 3.1.3.16)protein28131% helix, 35% strandQ4J6C0

Ligands and binding sites

  • MG · Magnesium ion · metal · 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
11110.400.7623empty
21230.400.7520empty

Interfaces

1 interface between chains.

  • A–B · 25 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

  • 2P8E · Crystal structure of the serine/threonine phosphatase domain of human PPM1B · the same entry in another collection · chain A against A, TM-score 1.00

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