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AlphaFold monomer V2.0 prediction for endonuclease 8-like 3 (Q8TAT5)

Analyse AlphaFold monomer V2.0 prediction for endonuclease 8-like 3 (Q8TAT5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q8TAT5
Type: protein
Length: 605 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
Molecule: Endonuclease 8-like 3
UniProt: Q8TAT5
Pockets: 5 · best druggability 0.72

Structure

1 distinct chain · 19% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endonuclease 8-like 3	protein	605	19% helix, 19% strand	Q8TAT5

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	838	0.72	0.77	87	empty
2	86	0.38	0.77	18	empty
3	59	0.33	0.77	13	empty
4	64	0.32	0.75	14	empty
5	54	0.30	0.76	13	empty

Compared structures

7JL5 · Crystal structure of human NEIL3 tandem zinc finger grf domains · an experimental structure of the same protein · chain A against B, TM-score 0.14
7JL5 · Crystal structure of human NEIL3 tandem zinc finger GRF domains · an experimental structure of the same protein · chain A against B, TM-score 0.14
7TMY · Structure of Mouse Importin alpha NEIL3 NLS Peptide Complex · an experimental structure of the same protein · chain A against A, TM-score 0.01

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 Q8TAT5
Elsewhere: UniProt Q8TAT5 · AlphaFold DB Q8TAT5

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