Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T68698 | Target Info | |||
| Target Name | Adenosylhomocysteinase (AHCY) | ||||
| Synonyms | SAHH; SAH hydrolase; S-adenosyl-L-homocysteine hydrolase | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | AHCY | ||||
| Biochemical Class | Ether bond hydrolase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Nicotinamide-Adenine-Dinucleotide | Ligand Info | |||
| Canonical SMILES | C1=CC(=C[N+](=C1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)N4C=NC5=C(N=CN=C54)N)O)O)O)O)C(=O)N | ||||
| InChI | 1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 | ||||
| InChIKey | BAWFJGJZGIEFAR-NNYOXOHSSA-N | ||||
| PubChem Compound ID | 5892 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 1LI4 Human S-adenosylhomocysteine hydrolase complexed with neplanocin | ||||||
| Method | X-ray diffraction | Resolution | 2.01 Å | Mutation | No | [1] |
| PDB Sequence |
DKLPYKVADI
12 GLAAWGRKAL22 DIAENEMPGL32 MRMRERYSAS42 KPLKGARIAG52 CLHMTVETAV 62 LIETLVTLGA72 EVQWSSCNIF82 STQDHAAAAI92 AKAGIPVYAW102 KGETDEEYLW 112 CIEQTLYFKD122 GPLNMILDDG132 GDLTNLIHTK142 YPQLLPGIRG152 ISEETTTGVH 162 NLYKMMANGI172 LKVPAINVND182 SVTKSKFDNL192 YGCRESLIDG202 IKRATDVMIA 212 GKVAVVAGYG222 DVGKGCAQAL232 RGFGARVIIT242 EIDPINALQA252 AMEGYEVTTM 262 DEACQEGNIF272 VTTTGCIDII282 LGRHFEQMKD292 DAIVCNIGHF302 DVEIDVKWLN 312 ENAVEKVNIK322 PQVDRYRLKN332 GRRIILLAEG342 RLVNLGCAMG352 HPSFVMSNSF 362 TNQVMAQIEL372 WTHPDKYPVG382 VHFLPKKLDE392 AVAEAHLGKL402 NVKLTKLTEK 412 QAQYLGMSCD422 GPFKPDHYRY432
|
|||||
|
|
THR157
2.594
THR158
2.725
THR159
2.628
HIS162
4.568
ASN181
4.776
LYS186
3.971
ASP190
3.428
ASN191
2.864
CYS195
4.091
ALA219
4.543
GLY220
3.620
TYR221
4.241
GLY222
3.365
ASP223
3.241
VAL224
2.950
GLY225
4.548
THR242
3.439
GLU243
2.719
|
|||||
| PDB ID: 4PFJ The structure of bi-acetylated SAHH | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | Yes | [2] |
| PDB Sequence |
DKLPYKVADI
12 GLAAWGRKAL22 DIAENEMPGL32 MRMRERYSAS42 KPLKGARIAG52 CLHMTVETAV 62 LIETLVTLGA72 EVQWSSCNIF82 STQNHAAAAI92 AKAGIPVYAW102 KGETDEEYLW 112 CIEQTLYFKD122 GPLNMILDDG132 GDLTNLIHTK142 YPQLLPGIRG152 ISEETTTGVH 162 NLYKMMANGI172 LKVPAINVND182 SVTKSKFDNL192 YGCRESLIDG202 IKRATDVMIA 212 GKVAVVAGYG222 DVGKGCAQAL232 RGFGARVIIT242 EIDPINALQA252 AMEGYEVTTM 262 DEACQEGNIF272 VTTTGCIDII282 LGRHFEQMKD292 DAIVCNIGHF302 DVEIDVKWLN 312 ENAVEKVNIK322 PQVDRYRLKN332 GRRIILLAEG342 RLVNLGCAMG352 HPSFVMSNSF 362 TNQVMAQIEL372 WTHPDKYPVG382 VHFLPKKLDE392 AVACAHLGLN403 VKLTLTEKQA 414 QYLGMSCDGP424 FKPDHYRY
|
|||||
|
|
THR157
2.243
THR158
1.953
THR159
1.983
GLY160
3.994
HIS162
4.405
ASN181
4.233
LYS186
3.073
ASP190
3.186
ASN191
2.480
CYS195
2.851
SER198
4.596
ALA219
3.670
GLY220
2.408
TYR221
2.673
GLY222
2.244
ASP223
2.639
VAL224
2.001
GLY225
3.537
THR242
2.449
GLU243
2.308
|
|||||
| PDB ID: 4PGF The structure of mono-acetylated SAHH | ||||||
| Method | X-ray diffraction | Resolution | 2.59 Å | Mutation | Yes | [2] |
| PDB Sequence |
DKLPYKVADI
12 GLAAWGRKAL22 DIAENEMPGL32 MRMRERYSAS42 KPLKGARIAG52 CLHMTVETAV 62 LIETLVTLGA72 EVQWSSCNIF82 STQNHAAAAI92 AKAGIPVYAW102 KGETDEEYLW 112 CIEQTLYFKD122 GPLNMILDDG132 GDLTNLIHTK142 YPQLLPGIRG152 ISEETTTGVH 162 NLYKMMANGI172 LKVPAINVND182 SVTKSKFDNL192 YGCRESLIDG202 IKRATDVMIA 212 GKVAVVAGYG222 DVGKGCAQAL232 RGFGARVIIT242 EIDPINALQA252 AMEGYEVTTM 262 DEACQEGNIF272 VTTTGCIDII282 LGRHFEQMKD292 DAIVCNIGHF302 DVEIDVKWLN 312 ENAVEKVNIK322 PQVDRYRLKN332 GRRIILLAEG342 RLVNLGCAMG352 HPSFVMSNSF 362 TNQVMAQIEL372 WTHPDKYPVG382 VHFLPKKLDE392 AVACAHLGKL402 NVKLTLTEKQ 413 AQYLGMSCDG423 PFKPDHYRY
|
|||||
|
|
THR157
1.872
THR158
2.453
THR159
1.981
GLY160
4.786
HIS162
3.702
ASN181
4.525
LYS186
2.850
ASP190
3.200
ASN191
2.428
CYS195
3.547
SER198
4.720
ALA219
3.555
GLY220
2.474
TYR221
2.909
GLY222
2.077
ASP223
2.623
VAL224
2.058
GLY225
3.577
THR242
2.626
GLU243
1.793
|
|||||
| PDB ID: 1A7A STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | Yes | [3] |
| PDB Sequence |
SDKLPYKVAD
11 IGLAAWGRKA21 LDIAENEPGL32 RRERYSASKP44 LKGARIAGCL54 HTVETAVLIE 65 TLVTLGAEVQ75 WSSCNIFSTQ85 NHAAAAIAKA95 GIPVYAWKGE105 TDEEYLWCIE 115 QTLYFKDGPL125 NILDDGGDLT136 NLIHTKYPQL146 LPGIRGISEE156 TTTGVHNLYK 166 ANGILKVPAI178 NVNDSVTKSK188 FDNLYGCRES198 LIDGIKRATD208 VIAGKVAVVA 219 GYGDVGKGCA229 QALRGFGARV239 IITEIDPINA249 LQAAEGYEVT260 TDEACQEGNI 271 FVTTTGCIDI281 ILGRHFEQKD292 DAIVCNIGHF302 DVEIDVKWLN312 ENAVEKVNIK 322 PQVDRYRLKN332 GRRIILLAEG342 RLVNLGCAGH353 PSFVSNSFTN364 QVAQIELWTH 375 PDKYPVGVHF385 LPKKLDEAVA395 EAHLGKLNVK405 LTKLTEKQAQ415 YLGSCDGPFK 426 PDHYRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:157 or .A:158 or .A:159 or .A:181 or .A:186 or .A:190 or .A:191 or .A:195 or .A:219 or .A:220 or .A:221 or .A:222 or .A:223 or .A:224 or .A:225 or .A:242 or .A:243 or .A:244 or .A:245 or .A:248 or .A:275 or .A:276 or .A:277 or .A:278 or .A:281 or .A:299 or .A:300 or .A:301 or .A:305 or .A:344 or .A:346 or .A:353; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
THR157
2.692
THR158
2.624
THR159
2.738
ASN181
4.868
LYS186
4.113
ASP190
3.699
ASN191
3.492
CYS195
4.206
ALA219
4.526
GLY220
3.477
TYR221
4.143
GLY222
2.731
ASP223
3.116
VAL224
2.717
GLY225
4.520
THR242
3.770
|
|||||
| PDB ID: 5W49 The crystal structure of human S-adenosylhomocysteine hydrolase (AHCY) bound to oxadiazole inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [4] |
| PDB Sequence |
KLPYKVADIG
13 LAAWGRKALD23 IAENEMPGLM33 RMRERYSASK43 PLKGARIAGC53 LHMTVETAVL 63 IETLVTLGAE73 VQWSSCNIFS83 TQDHAAAAIA93 KAGIPVYAWK103 GETDEEYLWC 113 IEQTLYFKDG123 PLNMILDDGG133 DLTNLIHTKY143 PQLLPGIRGI153 SEETTTGVHN 163 LYKMMANGIL173 KVPAINVNDS183 VTKSKFDNLY193 GCRESLIDGI203 KRATDVMIAG 213 KVAVVAGYGD223 VGKGCAQALR233 GFGARVIITE243 IDPINALQAA253 MEGYEVTTMD 263 EACQEGNIFV273 TTTGCIDIIL283 GRHFEQMKDD293 AIVCNIGHFD303 VEIDVKWLNE 313 NAVEKVNIKP323 QVDRYRLKNG333 RRIILLAEGR343 LVNLGCAMGH353 PSFVMSNSFT 363 NQVMAQIELW373 THPDKYPVGV383 HFLPKKLDEA393 VAEAHLGKLN403 VKLTKLTEKQ 413 AQYLGMSCDG423 PFKPDHYRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:190 or .A:191 or .A:195 or .A:219 or .A:220 or .A:221 or .A:222 or .A:223 or .A:224 or .A:225 or .A:242 or .A:243 or .A:244 or .A:245 or .A:248 or .A:275 or .A:276 or .A:277 or .A:278 or .A:279 or .A:281 or .A:299 or .A:300 or .A:301 or .A:305 or .A:344 or .A:346 or .A:347 or .A:353; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ASP190
3.366
ASN191
3.168
CYS195
3.832
ALA219
4.584
GLY220
3.710
TYR221
4.402
GLY222
3.293
ASP223
3.212
VAL224
2.886
GLY225
4.338
THR242
3.522
GLU243
2.767
ILE244
3.439
ASP245
3.439
ASN248
3.428
|
|||||
| PDB ID: 3NJ4 Fluoro-neplanocin A in Human S-Adenosylhomocysteine Hydrolase | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | No | [5] |
| PDB Sequence |
SDKLPYKVAD
11 IGLAAWGRKA21 LDIAENEMPG31 LMRMRERYSA41 SKPLKGARIA51 GCLHMTVETA 61 VLIETLVTLG71 AEVQWSSCNI81 FSTQDHAAAA91 IAKAGIPVYA101 WKGETDEEYL 111 WCIEQTLYFK121 DGPLNMILDD131 GGDLTNLIHT141 KYPQLLPGIR151 GISEETTTGV 161 HNLYKMMANG171 ILKVPAINVN181 DSVTKSKFDN191 LYGCRESLID201 GIKRATDVMI 211 AGKVAVVAGY221 GDVGKGCAQA231 LRGFGARVII241 TEIDPINALQ251 AAMEGYEVTT 261 MDEACQEGNI271 FVTTTGCIDI281 ILGRHFEQMK291 DDAIVCNIGH301 FDVEIDVKWL 311 NENAVEKVNI321 KPQVDRYRLK331 NGRRIILLAE341 GRLVNLGCAM351 GHPSFVMSNS 361 FTNQVMAQIE371 LWTHPDKYPV381 GVHFLPKKLD391 EAVAEAHLGK401 LNVKLTKLTE 411 KQAQYLGMSC421 DGPFKPDHYR431 Y
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:157 or .A:158 or .A:159 or .A:181 or .A:186 or .A:190 or .A:191 or .A:195 or .A:219 or .A:220 or .A:221 or .A:222 or .A:223 or .A:224 or .A:225 or .A:242 or .A:243 or .A:244 or .A:245 or .A:248 or .A:275 or .A:276 or .A:277 or .A:278 or .A:279 or .A:281 or .A:299 or .A:300 or .A:301 or .A:302 or .A:344 or .A:346 or .A:353; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
THR157
2.618
THR158
2.497
THR159
2.951
ASN181
4.889
LYS186
4.269
ASP190
3.692
ASN191
3.336
CYS195
4.140
ALA219
4.581
GLY220
3.621
TYR221
3.960
GLY222
3.105
ASP223
3.069
VAL224
2.819
GLY225
4.728
THR242
3.580
GLU243
2.664
|
|||||
| PDB ID: 5W4B The crystal structure of human S-adenosylhomocysteine hydrolase (AHCY) bound to benzothiazole inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 2.65 Å | Mutation | No | [4] |
| PDB Sequence |
LPYKVADIGL
14 AAWGRKALDI24 AENEMPGLMR34 MRERYSASKP44 LKGARIAGCL54 HMTVETAVLI 64 ETLVTLGAEV74 QWSSCNIFST84 QDHAAAAIAK94 AGIPVYAWKG104 ETDEEYLWCI 114 EQTLYFKDGP124 LNMILDDGGD134 LTNLIHTKYP144 QLLPGIRGIS154 EETTTGVHNL 164 YKMMANGILK174 VPAINVNDSV184 TKSKFDNLYG194 CRESLIDGIK204 RATDVMIAGK 214 VAVVAGYGDV224 GKGCAQALRG234 FGARVIITEI244 DPINALQAAM254 EGYEVTTMDE 264 ACQEGNIFVT274 TTGCIDIILG284 RHFEQMKDDA294 IVCNIGHFDV304 EIDVKWLNEN 314 AVEKVNIKPQ324 VDRYRLKNGR334 RIILLAEGRL344 VNLGCAMGHP354 SFVMSNSFTN 364 QVMAQIELWT374 HPDKYPVGVH384 FLPKKLDEAV394 AEAHLGKLNV404 KLTKLTEKQA 414 QYLGMSCDGP424 FKPDHYRY
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:158 or .A:190 or .A:191 or .A:195 or .A:219 or .A:220 or .A:221 or .A:222 or .A:223 or .A:224 or .A:225 or .A:242 or .A:243 or .A:244 or .A:245 or .A:248 or .A:275 or .A:276 or .A:277 or .A:278 or .A:281 or .A:299 or .A:300 or .A:301 or .A:344 or .A:346 or .A:347 or .A:353; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
THR158
4.103
ASP190
3.252
ASN191
2.683
CYS195
3.791
ALA219
4.735
GLY220
3.771
TYR221
4.356
GLY222
3.344
ASP223
3.213
VAL224
3.112
GLY225
4.567
THR242
3.492
GLU243
2.674
ILE244
3.588
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry. 2003 Feb 25;42(7):1900-9. | ||||
| REF 2 | Regulation of S-adenosylhomocysteine hydrolase by lysine acetylation. J Biol Chem. 2014 Nov 7;289(45):31361-72. | ||||
| REF 3 | Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol. 1998 May;5(5):369-76. | ||||
| REF 4 | Identification of AHCY inhibitors using novel high-throughput mass spectrometry. Biochem Biophys Res Commun. 2017 Sep 9;491(1):1-7. | ||||
| REF 5 | X-ray crystal structure and binding mode analysis of human S-adenosylhomocysteine hydrolase complexed with novel mechanism-based inhibitors, haloneplanocin A analogues. J Med Chem. 2011 Feb 24;54(4):930-8. | ||||
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