Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T78326 Target Info
Target Name N-acylethanolamine-hydrolyzing acidamidase (NAAA)
Synonyms Nacylsphingosine amidohydrolaselike; Nacylethanolaminehydrolyzing acid amidase subunit beta; NAAA; Acid ceramidaselike protein; ASAHlike protein
Target Type Literature-reported Target
Gene Name NAAA
Biochemical Class Carbon-nitrogen hydrolase
UniProt ID
NAAA_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: 2-{2-[4-(1,1,3,3-Tetramethylbutyl)phenoxy]ethoxy}ethanol Ligand Info
Structure Description Human N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of Triton X-100 PDB:6DXX
Method X-ray diffraction Resolution 2.70 Å Mutation No [1]
PDB Sequence
> Chain A
SPPAAPRFNV
38
SLDSVPELRW
48
LPVLRHYDLD
58
LVRAAMAQVI
68
GDRVPKWVHV
78

LIGKVVLELE
88
RFLPQPFTGE
98
IRGMCDFMNL
108
SLADCLLVNL
118
AYESSVF
> Chain B
CTSIVAQDSR
135
GHIYHGRNLD
145
YPFGNVLRKL
155
TVDVQFLKNG
165
QIAFTGTTFI
175

GYVGLWTGQS
185
PHKFTVSGDE
195
RDKGWWWENA
205
IAALFRRHIP
215
VSWLIRATLS
225

ESENFEAAVG
235
KLAKTPLIAD
245
VYYIVGGTSP
255
REGVVITRNR
265
DGPADIWPLD
275

PLNGAWFRVE
285
TNYDHWKPAP
295
KEDDRRTSAI
305
KALNATGQAN
315
LSLEALFQIL
325

SVVPVYNNFT
335
IYTTVMSAGS
345
PDKYMTRIRN
355
P
Residue
Distance (Å)
PRO73[A]
2.127
TRP75[A]
1.974
VAL76[A]
2.433
LEU79[A]
2.122
ILE80[A]
3.181
VAL83[A]
3.275
LEU87[A]
2.324
PHE90[A]
4.473
LEU115[A]
3.513
LEU118[A]
2.224
GLU121[A]
2.382
Residue
Distance (Å)
SER122[A]
2.268
SER123[A]
2.424
VAL124[A]
2.335
TRP201[B]
2.574
TRP202[B]
4.575
ASN204[B]
3.102
ALA205[B]
2.222
ALA208[B]
2.697
LEU209[B]
2.369
ILE243[B]
3.381
Ligand Name: [2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone Ligand Info
Structure Description Human N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of Triton X-100 PDB:6DXX
Method X-ray diffraction Resolution 2.70 Å Mutation No [1]
PDB Sequence
> Chain A
SPPAAPRFNV
38
SLDSVPELRW
48
LPVLRHYDLD
58
LVRAAMAQVI
68
GDRVPKWVHV
78

LIGKVVLELE
88
RFLPQPFTGE
98
IRGMCDFMNL
108
SLADCLLVNL
118
AYESSVF
> Chain B
CTSIVAQDSR
135
GHIYHGRNLD
145
YPFGNVLRKL
155
TVDVQFLKNG
165
QIAFTGTTFI
175

GYVGLWTGQS
185
PHKFTVSGDE
195
RDKGWWWENA
205
IAALFRRHIP
215
VSWLIRATLS
225

ESENFEAAVG
235
KLAKTPLIAD
245
VYYIVGGTSP
255
REGVVITRNR
265
DGPADIWPLD
275

PLNGAWFRVE
285
TNYDHWKPAP
295
KEDDRRTSAI
305
KALNATGQAN
315
LSLEALFQIL
325

SVVPVYNNFT
335
IYTTVMSAGS
345
PDKYMTRIRN
355
P
Residue
Distance (Å)
LEU59[A]
4.583
VAL60[A]
2.192
ARG61[A]
4.519
ALA63[A]
2.225
MET64[A]
2.378
VAL67[A]
3.453
MET106[A]
4.932
VAL116[A]
3.027
ASN117[A]
4.281
ALA119[A]
2.622
TYR120[A]
2.415
SER123[A]
4.756
PHE125[A]
2.732
CYS126[B]
3.429
ARG142[B]
4.081
Residue
Distance (Å)
LEU144[B]
3.256
ASP145[B]
3.104
TYR146[B]
3.004
LEU152[B]
3.063
LEU155[B]
2.822
PHE174[B]
2.492
ILE175[B]
2.576
GLY176[B]
3.040
TYR177[B]
2.617
TRP181[B]
2.380
GLY193[B]
4.055
ASP194[B]
3.751
GLU195[B]
2.286
VAL246[B]
4.619
ASN287[B]
4.582
References  Top
REF 1 Molecular mechanism of activation of the immunoregulatory amidase NAAA. Proc Natl Acad Sci U S A. 2018 Oct 23;115(43):E10032-E10040.

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