Research workbench

AlphaFold monomer V2.0 prediction for undecaprenyl- diphosphooligosaccharide--protein glycotransferase (Q5HTX9)

Analyse AlphaFold monomer V2.0 prediction for undecaprenyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q5HTX9
Type: protein
Length: 713 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x2823181CCd565C7bc2ae6FEB0337FEaA74b060D5
Molecule: Undecaprenyl-diphosphooligosaccharide--protein glycotransferase
UniProt: Q5HTX9
Pockets: 6 · best druggability 0.76

Structure

1 distinct chain · 59% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Undecaprenyl-diphosphooligosaccharide--protein glycotransferase	protein	713	59% helix, 12% strand	Q5HTX9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1194	0.76	0.78	102	empty
2	149	0.55	0.81	23	empty
3	156	0.49	0.77	24	empty
4	111	0.39	0.75	23	empty
5	81	0.34	0.75	20	empty

Compared structures

3AAG · Crystal structure of C. jejuni pglb C-terminal domain · an experimental structure of the same protein · chain A against A, TM-score 0.37
3AAG · Crystal structure of C. jejuni pglb C-terminal domain · an experimental structure of the same protein · chain A against A, TM-score 0.37

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 Q5HTX9
Elsewhere: UniProt Q5HTX9 · AlphaFold DB Q5HTX9

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