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Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity

Analyse Structure of PPM1, a leucine carboxy methyltransferase involved in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RJG
Type: protein
Length: 291 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxy methyl transferase for protein phosphatase 2A catalytic subunit
EC: 2.1.1.-
UniProt: Q04081
Ligands: SAH
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxy methyl transferase for protein phosphatase 2A catalytic subunit (EC 2.1.1.-)	protein	291	52% helix, 17% strand	Q04081

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	361	0.68	0.81	54	SAH

Compared structures

1RJG · Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of… · the same entry in another collection · chain A against A, TM-score 1.00
Q04081 · AlphaFold monomer V2.0 prediction for leucine carboxyl methyltransferase 1 (Q04081) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q04081
Elsewhere: RCSB PDB 1RJG · PDBe 1RJG · UniProt Q04081

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