MolNFT v1 · #11219 · protein

Crystal structure of L-isoaspartyl (D-aspartyl) O- methyltransferase with S-adenosylmethionine

1JG4 · Protein-L-isoaspartate O-methyltransferase: “Crystal structure of L-isoaspartyl (D-aspartyl) O- methyltransferase with S-adenosylmethionine”. X-ray diffraction, 1 ligand (SAM), 1 pocket (best druggability 0.70). MolNFT v1 #11219 on…

PDB: 1JG4
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-L-isoaspartate O-methyltransferase
EC: 2.1.1.77
UniProt: Q8TZR3
Ligands: SAM
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-L-isoaspartate O-methyltransferase (EC 2.1.1.77)	protein	215	39% helix, 28% strand	Q8TZR3

Ligands and binding sites

SAM · S-adenosylmethionine · 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	190	0.70	0.87	40	SAM

Compared structures

1JG4 · Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with… · the same entry in another collection · chain A against A, TM-score 1.00
Q8TZR3 · AlphaFold monomer V2.0 prediction for protein-L-isoaspartate O-methyltransferase (Q8TZR3) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q8TZR3
Elsewhere: RCSB PDB 1JG4 · PDBe 1JG4 · UniProt Q8TZR3

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