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AlphaFold monomer V2.0 prediction for udp-4-amino-4,6-dideoxy-N- acetyl-beta-L-altrosamine N-acetyltransferase (O25094)

Analyse AlphaFold monomer V2.0 prediction for udp-4-amino-4,6-dideoxy-N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: O25094
Type: protein
Length: 180 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x8216949dDEF9EaDBdB1a9037895912E009a911AA
Molecule: Udp-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase
UniProt: O25094
Pockets: 2 · best druggability 0.73

Structure

1 distinct chain · 35% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase	protein	180	35% helix, 36% strand	O25094

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	566	0.73	0.81	44	empty
2	80	0.38	0.77	19	empty

Compared structures

4RI1 · Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N… · an experimental structure of the same protein · chain A against A, TM-score 0.98
4RI1 · Crystal structure of helicobacter pylori pseudaminic acid biosynthesis N… · an experimental structure of the same protein · chain A against A, TM-score 0.98

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 O25094
Elsewhere: UniProt O25094 · AlphaFold DB O25094

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