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AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase (P60753)

Analyse AlphaFold monomer V2.0 prediction for ATP-dependent lipid a-core flippase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P60753
Type: protein
Length: 582 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
Molecule: ATP-dependent lipid a-core flippase
UniProt: P60753
Pockets: 8 · best druggability 0.62

Structure

1 distinct chain · 66% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent lipid a-core flippase	protein	582	66% helix, 10% strand	P60753

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	424	0.62	0.76	44	empty
2	127	0.61	0.85	23	empty
3	195	0.48	0.75	20	empty
4	89	0.40	0.77	16	empty
5	91	0.37	0.75	18	empty

Compared structures

5TV4 · 3D cryo-EM reconstruction of nucleotide-free MsbA in lipid nanodisc · an experimental structure of the same protein · chain A against A, TM-score 0.86
5TV4 · 3D cryo-EM reconstruction of nucleotide-free msba in lipid nanodisc · an experimental structure of the same protein · chain A against A, TM-score 0.86
5TTP · Cryo-EM structure of msba-nanodisc with ADP-vanadate · an experimental structure of the same protein · chain A against A, TM-score 0.68

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 P60753
Elsewhere: UniProt P60753 · AlphaFold DB P60753

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