Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T46318 | Target Info | |||
| Target Name | Acyloxyacyl hydrolase (neutrophil) | ||||
| Synonyms | Acyloxyacyl hydrolase | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | AOAH | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Lauric acid | Ligand Info | |||||
| Structure Description | Human acyloxyacyl hydrolase (AOAH), proteolytically processed, S263A mutant, with LPS | PDB:5W7C | ||||
| Method | X-ray diffraction | Resolution | 2.23 Å | Mutation | Yes | [1] |
| PDB Sequence |
GSDICSLPVL
165 AKICQKIKLA175 MEQSVPFKDV185 DSDKYSVFPT195 LRGYHWRGRD205 CNDSDESVYP 215 GRRPNNWDVH225 QDSNCNGIWG235 VDPKDGVPYE245 KKFCEGSQPR255 GIILLGDAAG 265 AHFHISPEWI275 TASQMSLNSF285 INLPTALTNE295 LDWPQLSGAT305 GFLDSTVGIK 315 EKSIYLRLWK325 RNHCNHRDYQ335 NISRNGASSR345 NLKKFIESLS355 RNKVLDYPAI 365 VIYAMIGNDV375 CSGKSDPVPA385 MTTPEKLYSN395 VMQTLKHLNS405 HLPNGSHVIL 415 YGLPDGTFLW425 DNLHNRYHPL435 GQLNKDMTYA445 QLYSFLNCLQ455 VSPCHGWMSS 465 NKTLRTLTSE475 RAEQLSNTLK485 KIAASEKFTN495 FNLFYMDFAF505 HEIIQEWQKR 515 GGQPWQLIEP525 VDGFHPNEVA535 LLLLADHFWK545 KVQLQWPQIL555 GKENPFNPQI 565 KQVFGDQGGH575
|
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|
|
ASP262
2.975
ALA263
2.888
ALA264
2.293
GLY265
4.628
PHE268
4.798
ASN340
2.687
GLY341
3.613
ILE371
2.367
GLY372
2.693
ASN373
2.327
CYS376
3.220
PRO419
2.435
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Myristic acid | Ligand Info | |||||
| Structure Description | Human acyloxyacyl hydrolase (AOAH), proteolytically processed | PDB:5W78 | ||||
| Method | X-ray diffraction | Resolution | 2.27 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
LSNGHTCVGC 44 VLVVSVIEQL54 AQVHNSTVQA64 SMERLCSYLP74 EKLFLKTTCY84 LVIDKFGSDI 94 IKLLSADMNA104 DVVCHTLEFC114 KQNTGQPLCH124 LYPLPKETWK134 FTLQKARQIV 144 KKSPILKY> Chain B DICSLPVLAK 167 ICQKIKLAME177 QSVFPTLRGY199 HWRGRDCNDS209 DESVYPGRRP219 NNWDVHQDSN 229 CNGIWGVDPK239 DGVPYEKKFC249 EGSQPRGIIL259 LGDSAGAHFH269 ISPEWITASQ 279 MSLNSFINLP289 TALTNELDWP299 QLSGATGFLD309 STVGIKEKSI319 YLRLWKRNHC 329 NHRDYQNISR339 NGASSRNLKK349 FIESLSRNKV359 LDYPAIVIYA369 MIGNDVCSGK 379 SDPVPAMTTP389 EKLYSNVMQT399 LKHLNSHLPN409 GSHVILYGLP419 DGTFLWDNLH 429 NRYHPLGQLN439 KDMTYAQLYS449 FLNCLQVSPC459 HGWMSSNKTL469 RTLTSERAEQ 479 LSNTLKKIAA489 SEKFTNFNLF499 YMDFAFHEII509 QEWQKRGGQP519 WQLIEPVDGF 529 HPNEVALLLL539 ADHFWKKVQL549 QWPQILGKEN559 PFNPQIKQVF569 GDQGGH |
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GLY38[A]
4.989
HIS39[A]
2.915
THR40[A]
4.400
VAL42[A]
2.188
GLY43[A]
1.873
CYS44[A]
2.832
LEU46[A]
2.909
VAL47[A]
2.122
VAL48[A]
3.218
ILE51[A]
2.392
MET66[A]
2.498
GLU67[A]
4.868
LEU69[A]
2.122
CYS70[A]
3.068
LEU73[A]
2.798
LEU79[A]
2.727
THR82[A]
2.812
CYS83[A]
2.641
TYR84[A]
4.773
VAL86[A]
2.300
ILE87[A]
2.371
PHE90[A]
2.896
ILE94[A]
2.590
LEU111[A]
3.911
PHE113[A]
2.531
ILE159[B]
2.473
CYS160[B]
4.247
LEU162[B]
2.553
VAL164[B]
4.080
LEU165[B]
2.493
ILE168[B]
2.912
CYS169[B]
3.890
ILE172[B]
2.653
LEU288[B]
3.685
LEU292[B]
2.550
VAL456[B]
4.458
|
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| Ligand Name: 3-Hydroxytetradecanoic acid | Ligand Info | |||||
| Structure Description | Human acyloxyacyl hydrolase (AOAH), proteolytically processed, S263A mutant, with LPS | PDB:5W7C | ||||
| Method | X-ray diffraction | Resolution | 2.23 Å | Mutation | Yes | [1] |
| PDB Sequence |
> Chain A
LSNGHTCVGC 44 VLVVSVIEQL54 AQVHNSTVQA64 SMERLCSYLP74 EKLFLKTTCY84 LVIDKFGSDI 94 IKLLSADMNA104 DVVCHTLEFC114 KQNTGQPLCH124 LYPLPKETWK134 FTLQKARQIV 144 K> Chain C GSDICSLPVL 165 AKICQKIKLA175 MEQSVPFKDV185 DSDKYSVFPT195 LRGYHWRGRD205 CNDSDESVYP 215 GRRPNNWDVH225 QDSNCNGIWG235 VDPKDGVPYE245 KKFCEGSQPR255 GIILLGDAAG 265 AHFHISPEWI275 TASQMSLNSF285 INLPTALTNE295 LDWPQLSGAT305 GFLDSTVGIK 315 EKSIYLRLWK325 RNHCNHRDYQ335 NISRNGASSR345 NLKKFIESLS355 RNKVLDYPAI 365 VIYAMIGNDV375 CSGKSDPVPA385 MTTPEKLYSN395 VMQTLKHLNS405 HLPNGSHVIL 415 YGLPDGTFLW425 DNLHNRYHPL435 GQLNKDMTYA445 QLYSFLNCLQ455 VSPCHGWMSS 465 NKTLRTLTSE475 RAEQLSNTLK485 KIAASEKFTN495 FNLFYMDFAF505 HEIIQEWQKR 515 GGQPWQLIEP525 VDGFHPNEVA535 LLLLADHFWK545 KVQLQWPQIL555 GKENPFNPQI 565 KQVFGDQGGH575
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FTT or .FTT2 or .FTT3 or :3FTT;style chemicals stick;color identity;select .A:39 or .A:42 or .A:46 or .A:47 or .A:50 or .A:69 or .A:73 or .A:37 or .A:39 or .A:40 or .A:43 or .A:44 or .A:47 or .A:48 or .A:51 or .A:86 or .A:90 or .A:94 or .A:111 or .A:113 or .C:263 or .C:268 or .C:270 or .C:274 or .C:275 or .C:280 or .C:285 or .C:288 or .C:292 or .C:296 or .C:340 or .C:341 or .C:373 or .C:433 or .C:435 or .C:447 or .C:451 or .C:456 or .C:457 or .C:458 or .C:463 or .C:526 or .C:527 or .C:529 or .C:530; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS39[A]
4.710
VAL42[A]
2.273
LEU46[A]
2.730
VAL47[A]
3.289
VAL50[A]
2.796
LEU69[A]
3.054
LEU73[A]
3.543
ASN37[A]
3.973
HIS39[A]
2.491
THR40[A]
2.395
GLY43[A]
2.374
CYS44[A]
2.555
VAL47[A]
2.226
VAL48[A]
3.259
ILE51[A]
4.871
VAL86[A]
2.874
PHE90[A]
3.665
ILE94[A]
2.890
LEU111[A]
4.695
PHE113[A]
2.997
ALA263[C]
2.908
PHE268[C]
2.435
ILE270[C]
2.176
TRP274[C]
2.563
ILE275[C]
2.778
MET280[C]
4.038
PHE285[C]
2.271
LEU288[C]
3.772
LEU292[C]
3.712
LEU296[C]
2.358
ASN340[C]
2.288
GLY341[C]
2.660
ASN373[C]
4.200
HIS433[C]
3.611
LEU435[C]
4.219
LEU447[C]
2.949
LEU451[C]
2.894
VAL456[C]
3.895
SER457[C]
4.631
PRO458[C]
2.308
MET463[C]
4.271
VAL526[C]
3.184
ASP527[C]
2.859
PHE529[C]
4.812
HIS530[C]
2.206
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal structure of the mammalian lipopolysaccharide detoxifier. Proc Natl Acad Sci U S A. 2018 Jan 30;115(5):E896-E905. | ||||
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