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AlphaFold monomer V2.0 prediction for N-acylethanolamine-hydrolyzing acid amidase (Q9GUI1)

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

Accession: Q9GUI1
Type: protein
Length: 355 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x81FFd8C96E4A5454E3d65dFf78C1042d8fF7DAdA
Molecule: N-acylethanolamine-hydrolyzing acid amidase
UniProt: Q9GUI1
Pockets: 5 · best druggability 0.82

Structure

1 distinct chain · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acylethanolamine-hydrolyzing acid amidase	protein	355	37% helix, 24% strand	Q9GUI1

Pockets

5 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	153	0.82	0.97	28	empty
2	248	0.60	0.79	30	empty
3	71	0.46	0.83	14	empty
4	134	0.43	0.76	22	empty
5	101	0.39	0.76	20	empty

Compared structures

6DY3 · Caenorhabditis elegans N-acylethanolamine-hydrolyzing acid amidase (NAAA) ortholog · an experimental structure of the same protein · chain A against H, TM-score 0.62
6DY3 · Caenorhabditis elegans N-acylethanolamine-hydrolyzing acid amidase (naaa) ortholog · an experimental structure of the same protein · chain A against B, TM-score 0.62

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 Q9GUI1
Elsewhere: UniProt Q9GUI1 · AlphaFold DB Q9GUI1

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