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AlphaFold monomer V2.0 prediction for glycerol-3-phosphate cytidylyltransferase (P27623)

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

Accession: P27623
Type: protein
Length: 129 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xAA02A2FF70d56DfE0213584307973a4Afb1e909E
Molecule: Glycerol-3-phosphate cytidylyltransferase
UniProt: P27623
Pockets: 1 · best druggability 0.66

Structure

1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycerol-3-phosphate cytidylyltransferase	protein	129	38% helix, 22% strand	P27623

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	250	0.66	0.83	34	empty

Compared structures

1COZ · CTP:GLYCEROL-3-phosphate cytidylyltransferase from bacillus subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.96
1COZ · CTP:GLYCEROL-3-phosphate cytidylyltransferase from bacillus subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.96
1N1D · Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol · an experimental structure of the same protein · chain A against A, TM-score 0.96
1N1D · Glycerol-3-phosphate cytidylyltransferase complexed with cdp-glycerol · an experimental structure of the same protein · chain A against A, TM-score 0.96

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 P27623
Elsewhere: UniProt P27623 · AlphaFold DB P27623

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