N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (ACY3)

Homo sapiens — UniProt Q96HD9

Gene: ACY3Homo sapiensSwissProt reviewed

About N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (ACY3) is a protein from Homo sapiens identified by UniProt accession Q96HD9, 319 residues long. MolForge cross-references it against 0 known binders and 55 disease associations.

Target properties

Protein nameN-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
UniProt accessionQ96HD9
GeneACY3
OrganismHomo sapiens
Length319 residues
Molecular weight—
EC numbers—
Target classUNCLASSIFIED
Subcellular location—
Keywords—

Druggability

Target tractability assessment (Open Targets + pocket analysis). No approved drug

Druggability tierMEDIUM
Druggability score—
Pocket score—
Max clinical phase—

Disease associations (55)

Diseases linked to this target (Open Targets).

  • serum metabolite measurement · score 0.43
  • neurodegenerative disease · score 0.38
  • urinary metabolite measurement · score 0.37
  • lysosomal storage disease · score 0.34
  • Alzheimer disease · score 0.34
  • multiple sclerosis · score 0.34
  • Parkinson disease · score 0.34
  • glioblastoma multiforme · score 0.13
  • Barrett's esophagus · score 0.07
  • hemoglobin E-beta-thalassemia syndrome · score 0.05

3D Structure (1)

Experimental (PDB) and predicted (AlphaFold) structures for this protein.

StructureSourceMethodMean pLDDTResolution (Å)
AF-Q96HD9-F1alphafoldPREDICTED95.29—

Amino-acid sequence (319 residues)

MCSLPVPREP LRRVAVTGGT HGNEMSGVYL ARHWLHAPAE LQRASFSAVP VLANPAATSG CRRYVDHDLN RTFTSSFLNS RPTPDDPYEV TRARELNQLL GPKASGQAFD FVLDLHNTTA NMGTCLIAKS SHEVFAMHLC RHLQLQYPEL SCQVFLYQRS GEESYNLDSV AKNGLGLELG PQPQGVLRAD IFSRMRTLVA TVLDFIELFN QGTAFPAFEM EAYRPVGVVD FPRTEAGHLA GTVHPQLQDR DFQPLQPGAP IFQMFSGEDL LYEGESTVYP VFINEAAYYE KGVAFVQTEK FTFTVPAMPA LTPAPSPAS

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Quick facts

UniProtQ96HD9
GeneACY3
OrganismHomo sapiens
Length319
Binders0
Diseases55
View on UniProt