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AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase subunit gamma (A7MAS3)

Analyse AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: A7MAS3
Type: protein
Length: 351 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
Molecule: ATP-dependent 6-phosphofructokinase subunit gamma
UniProt: A7MAS3
Pockets: 6 · best druggability 0.77

Structure

1 distinct chain · 43% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent 6-phosphofructokinase subunit gamma	protein	351	43% helix, 7% strand	A7MAS3

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1055	0.77	0.78	86	empty
2	88	0.53	0.84	21	empty
3	101	0.51	0.82	18	empty
4	151	0.47	0.76	18	empty
5	73	0.36	0.77	13	empty

Compared structures

3OPY · Crystal structure of Pichia pastoris phosphofructokinase in the T-state · an experimental structure of the same protein · chain A against I, TM-score 0.42
3OPY · Crystal structure of pichia pastoris phosphofructokinase in the T- state · an experimental structure of the same protein · chain A against I, TM-score 0.42

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 A7MAS3
Elsewhere: UniProt A7MAS3 · AlphaFold DB A7MAS3

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