Research workbench

AlphaFold monomer V2.0 prediction for teichoic acids export ATP- binding protein tagh (P42954)

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: P42954
Type: protein
Length: 527 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x3c673E4E26fFbBb142D38f43b99Bd7D21c3AABD8
Molecule: Teichoic acids export ATP-binding protein tagh
UniProt: P42954
Pockets: 5 · best druggability 0.54

Structure

1 distinct chain · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Teichoic acids export ATP-binding protein tagh	protein	527	34% helix, 29% strand	P42954

Pockets

5 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	177	0.54	0.79	29	empty
2	79	0.48	0.83	20	empty
3	58	0.35	0.77	12	empty
4	65	0.33	0.76	16	empty
5	54	0.28	0.75	17	empty

Compared structures

7DD0 · Crystal structure of the N-terminal domain of tagh from bacillus subtilis · an experimental structure of the same protein · chain A against B, TM-score 0.46
7DD0 · Crystal structure of the N-terminal domain of TagH from Bacillus subtilis · an experimental structure of the same protein · chain A against B, TM-score 0.46

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 P42954
Elsewhere: UniProt P42954 · AlphaFold DB P42954

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