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AlphaFold monomer V2.0 prediction for inactive tyrosine-protein kinase PEAK1 (Q9H792)

Analyse AlphaFold monomer V2.0 prediction for inactive tyrosine-protein kinase PEAK1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9H792
Type: protein
Length: 1,746 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
Molecule: Inactive tyrosine-protein kinase PEAK1
UniProt: Q9H792
Pockets: 10 · best druggability 0.64

Structure

1 distinct chain · 16% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inactive tyrosine-protein kinase PEAK1	protein	1746	16% helix, 4% strand	Q9H792

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	498	0.64	0.77	45	empty
2	327	0.60	0.77	35	empty
3	184	0.57	0.81	21	empty
4	279	0.56	0.77	23	empty
5	253	0.50	0.74	28	empty

Compared structures

6BHC · Crystal structure of pseduokinase PEAK1 (sugen kinase 269) · an experimental structure of the same protein · chain A against A, TM-score 0.21
6BHC · Crystal structure of pseduokinase PEAK1 (Sugen Kinase 269) · an experimental structure of the same protein · chain A against A, TM-score 0.21
8DGM · 14-3-3 epsilon bound to phosphorylated PEAK1 (pT1165) peptide · an experimental structure of the same protein · chain A against B, TM-score 0.00

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 Q9H792
Elsewhere: UniProt Q9H792 · AlphaFold DB Q9H792

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