MolNFT v1 · #418555 · protein

AlphaFold monomer V2.0 prediction for bifunctional sugar-1-phosphate NUCLEOTIDYLYLTRANSFERASE/ACETYLTRANSFERASE (Q975F9)

Q975F9: “AlphaFold monomer V2.0 prediction for bifunctional sugar-1-phosphate…”. 2 pockets (best druggability 0.76). MolNFT v1 #418555 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: Q975F9
Type: protein
Length: 401 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
Molecule: Bifunctional sugar-1-phosphate NUCLEOTIDYLYLTRANSFERASE/ACETYLTRANSFERASE
UniProt: Q975F9
Pockets: 2 · best druggability 0.76

Structure

1 distinct chain · 18% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional sugar-1-phosphate NUCLEOTIDYLYLTRANSFERASE/ACETYLTRANSFERASE	protein	401	18% helix, 35% strand	Q975F9

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	690	0.76	0.82	67	empty
2	67	0.32	0.75	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5Z09 · ST0452(Y97N)-UTP binding form · an experimental structure of the same protein · chain A against A, TM-score 0.99
5Z0A · ST0452(Y97N)-glcnac binding form · an experimental structure of the same protein · chain A against A, TM-score 0.99

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 Q975F9
Elsewhere: UniProt Q975F9 · AlphaFold DB Q975F9

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