Research workbench

O-glcnac transferase tpr domain with the intellectual disability associated mutation L254F

Analyse O-glcnac transferase tpr domain with the intellectual disability associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EOU
Type: protein
Length: 343 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda subunit
EC: 2.4.1.255
UniProt: O15294
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda subunit (EC 2.4.1.255)	protein	343	80% helix, 0% strand	O15294

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.28	0.74	13	empty

Compared structures

6EOU · O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F · the same entry in another collection · chain A against A, TM-score 1.00
O15294 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide… · a predicted model of the same protein · chain A against A, TM-score 0.82

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 O15294
Elsewhere: RCSB PDB 6EOU · PDBe 6EOU · UniProt O15294

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.