Research workbench

AlphaFold monomer V2.0 prediction for N-acylethanolamine-hydrolyzing acid amidase (Q9D7V9)

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: Q9D7V9
Type: protein
Length: 362 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xC3139F25753039810c47bBeCF44703fF28C29Fd6
Molecule: N-acylethanolamine-hydrolyzing acid amidase
UniProt: Q9D7V9

Structure

1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acylethanolamine-hydrolyzing acid amidase	protein	362	34% helix, 24% strand	Q9D7V9

Compared structures

6DXY · Murine N-acylethanolamine-hydrolyzing acid amidase (NAAA) · an experimental structure of the same protein · chain A against D, TM-score 0.63
6DXY · Murine N-acylethanolamine-hydrolyzing acid amidase (naaa) · an experimental structure of the same protein · chain A against B, TM-score 0.63

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 Q9D7V9
Elsewhere: UniProt Q9D7V9 · AlphaFold DB Q9D7V9

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