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AlphaFold monomer V2.0 prediction for eca polysaccharide chain length modulation protein (P0AG00)

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

Accession: P0AG00
Type: protein
Length: 348 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
Molecule: Eca polysaccharide chain length modulation protein
UniProt: P0AG00
Pockets: 1 · best druggability 0.31

Structure

1 distinct chain · 65% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eca polysaccharide chain length modulation protein	protein	348	65% helix, 7% strand	P0AG00

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.31	0.76	17	empty

Compared structures

8P3P · Full-length bacterial polysaccharide co-polymerase WzzE mutant R267E from E. coli. C4… · an experimental structure of the same protein · chain A against H, TM-score 0.91
8BHW · Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C4 symmetry · an experimental structure of the same protein · chain A against H, TM-score 0.91
8P3O · Full-length bacterial polysaccharide co-polymerase WzzE mutant R267A from E. coli. C4… · an experimental structure of the same protein · chain A against B, TM-score 0.88

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 P0AG00
Elsewhere: UniProt P0AG00 · AlphaFold DB P0AG00

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