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Crystal structure of gtb C80S/C196S/C209S + udp + H antigen

Analyse Crystal structure of gtb C80S/C196S/C209S + udp + H antigen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I0K
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Abo glycosyltransferase
EC: 2.4.1.37
UniProt: Q70V26
Ligands: BHG, UDP, FUC
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Abo glycosyltransferase (EC 2.4.1.37)	protein	267	33% helix, 21% strand	Q70V26

Ligands and binding sites

BHG · hexyl beta-D-galactopyranoside · ligand · chains A
UDP · Uridine-5'-diphosphate · ligand · chains A
FUC · alpha-L-fucopyranose · sugar · 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	331	0.62	0.79	37	BHG, FUC, UDP

Compared structures

3I0K · Crystal structure of GTB C80S/C196S/C209S + UDP + H antigen · 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 Q70V26
Elsewhere: RCSB PDB 3I0K · PDBe 3I0K · UniProt Q70V26

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