Research workbench

Chimeric glycosyltransferase LANGT2S8AC

Analyse Chimeric glycosyltransferase LANGT2S8AC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RIG
Type: protein
Length: 703 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl transferase
UniProt: Q9ZGC0, Q9RPA7
Ligands: MG
Pockets: 9 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl transferase	protein	344	43% helix, 16% strand	Q9ZGC0, Q9RPA7
B	Glycosyl transferase	protein	359	46% helix, 15% strand	Q9ZGC0, Q9RPA7

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains B

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	717	0.74	0.80	64	empty
2	698	0.73	0.79	61	empty
3	64	0.70	0.97	26	empty
4	168	0.59	0.82	27	empty
5	153	0.58	0.82	24	empty

Interfaces

1 interface between chains.

A–B · 1523 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4RIG · Chimeric Glycosyltransferase LanGT2S8Ac · the same entry in another collection · 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 Q9ZGC0
Every structure of UniProt Q9RPA7
Elsewhere: RCSB PDB 4RIG · PDBe 4RIG · UniProt Q9ZGC0 · UniProt Q9RPA7

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