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AlphaFold monomer V2.0 prediction for teichoic acids export ATP- binding protein tagh (Q88ZH4)

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

Accession: Q88ZH4
Type: protein
Length: 363 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xb3371708538E23D29A3Bd51b2aAF1CBe50bF8768
Molecule: Teichoic acids export ATP-binding protein tagh
UniProt: Q88ZH4
Pockets: 1 · best druggability 0.48

Structure

1 distinct chain · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Teichoic acids export ATP-binding protein tagh	protein	363	50% helix, 18% strand	Q88ZH4

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	87	0.48	0.82	25	empty

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 Q88ZH4
Elsewhere: UniProt Q88ZH4 · AlphaFold DB Q88ZH4

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