Research workbench

Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L- homocysteine

Analyse Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L- homocysteine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R18
Type: protein
Length: 223 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-L-ISOASPARTATE(D-aspartate)-O-methyltransferase
EC: 2.1.1.77
UniProt: Q27869
Ligands: SAH
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-L-ISOASPARTATE(D-aspartate)-O-methyltransferase (EC 2.1.1.77)	protein	223	34% helix, 27% strand	Q27869

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	486	0.74	0.83	58	SAH

Compared structures

1R18 · Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L-homocysteine · the same entry in another collection · chain A against A, TM-score 1.00
Q27869 · AlphaFold monomer V2.0 prediction for protein-L- ISOASPARTATE(D-aspartate)… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q27869
Elsewhere: RCSB PDB 1R18 · PDBe 1R18 · UniProt Q27869

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