Research workbench

Crystal structure of N-acetylglucosaminyltransferase I

Analyse Crystal structure of N-acetylglucosaminyltransferase I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FO9
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-1,3-mannosyl-glycoprotein beta-1,2-N- acetylglucosaminyltransferase
EC: 2.4.1.101
UniProt: P27115
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1,3-mannosyl-glycoprotein beta-1,2-N- acetylglucosaminyltransferase (EC 2.4.1.101)	protein	331	35% helix, 21% strand	P27115

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.53	0.76	35	empty
2	88	0.36	0.75	15	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1FO9 · Crystal structure of N-acetylglucosaminyltransferase I · the same entry in another collection · chain A against A, TM-score 1.00
P27115 · AlphaFold monomer V2.0 prediction for alpha-1,3-mannosyl-glycoprotein… · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P27115
Elsewhere: RCSB PDB 1FO9 · PDBe 1FO9 · UniProt P27115

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