Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T44282 | Target Info | |||
| Target Name | Mitochondrial aldehyde dehydrogenase (ALDH2) | ||||
| Synonyms | Aldehyde dehydrogenase, mitochondrial; ALDM; ALDHI; ALDH-E2; ALDH class 2 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | ALDH2 | ||||
| Biochemical Class | Aldehyde/oxo donor oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | NADH | Ligand Info | |||
| Canonical SMILES | C1C=CN(C=C1C(=O)N)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 | ||||
| InChI | 1S/C21H29N7O14P2/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/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 | ||||
| InChIKey | BOPGDPNILDQYTO-NNYOXOHSSA-N | ||||
| PubChem Compound ID | 439153 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 1O02 Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of Mg2+ | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [1] |
| PDB Sequence |
AVPAPNQQPE
16 VFCNQIFINN26 EWHDAVSRKT36 FPTVNPSTGE46 VICQVAEGDK56 EDVDKAVKAA 66 RAAFQLGSPW76 RRMDASHRGR86 LLNRLADLIE96 RDRTYLAALE106 TLDNGKPYVI 116 SYLVDLDMVL126 KCLRYYAGWA136 DKYHGKTIPI146 DGDFFSYTRH156 EPVGVCGQII 166 PWNFPLLMQA176 WKLGPALATG186 NVVVMKVAEQ196 TPLTALYVAN206 LIKEAGFPPG 216 VVNIVPGFGP226 TAGAAIASHE236 DVDKVAFTGS246 TEIGRVIQVA256 AGSSNLKRVT 266 LELGGKSPNI276 IMSDADMDWA286 VEQAHFALFF296 NQGQCCCAGS306 RTFVQEDIYD 316 EFVERSVARA326 KSRVVGNPFD336 SKTEQGPQVD346 ETQFKKILGY356 INTGKQEGAK 366 LLCGGGIAAD376 RGYFIQPTVF386 GDVQDGMTIA396 KEEIFGPVMQ406 ILKFKTIEEV 416 VGRANNSTYG426 LAAAVFTKDL436 DKANYLSQAL446 QAGTVWVNCY456 DVFGAQSPFG 466 GYKMSGSGRE476 LGEYGLQAYT486 EVKTVTVKVP496 QKNS
|
|||||
|
|
ILE165
3.464
ILE166
2.851
PRO167
3.353
TRP168
2.881
ASN169
3.091
LYS192
2.776
VAL193
4.230
ALA194
3.712
GLU195
2.815
GLN196
3.904
GLY223
4.560
PHE224
4.030
GLY225
3.278
PRO226
3.743
GLY229
3.225
ALA230
3.323
|
|||||
| PDB ID: 1NZZ Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of low Mg2+ | ||||||
| Method | X-ray diffraction | Resolution | 2.45 Å | Mutation | No | [1] |
| PDB Sequence |
AVPAPNQQPE
16 VFCNQIFINN26 EWHDAVSRKT36 FPTVNPSTGE46 VICQVAEGDK56 EDVDKAVKAA 66 RAAFQLGSPW76 RRMDASHRGR86 LLNRLADLIE96 RDRTYLAALE106 TLDNGKPYVI 116 SYLVDLDMVL126 KCLRYYAGWA136 DKYHGKTIPI146 DGDFFSYTRH156 EPVGVCGQII 166 PWNFPLLMQA176 WKLGPALATG186 NVVVMKVAEQ196 TPLTALYVAN206 LIKEAGFPPG 216 VVNIVPGFGP226 TAGAAIASHE236 DVDKVAFTGS246 TEIGRVIQVA256 AGSSNLKRVT 266 LELGGKSPNI276 IMSDADMDWA286 VEQAHFALFF296 NQGQCCCAGS306 RTFVQEDIYD 316 EFVERSVARA326 KSRVVGNPFD336 SKTEQGPQVD346 ETQFKKILGY356 INTGKQEGAK 366 LLCGGGIAAD376 RGYFIQPTVF386 GDVQDGMTIA396 KEEIFGPVMQ406 ILKFKTIEEV 416 VGRANNSTYG426 LAAAVFTKDL436 DKANYLSQAL446 QAGTVWVNCY456 DVFGAQSPFG 466 GYKMSGSGRE476 LGEYGLQAYT486 EVKTVTVKVP496 QKNS
|
|||||
|
|
ILE165
3.403
ILE166
3.224
PRO167
3.228
TRP168
2.858
ASN169
3.002
LYS192
2.837
VAL193
4.026
ALA194
3.701
GLU195
2.753
GLN196
3.873
GLY223
4.468
PHE224
3.990
GLY225
3.227
PRO226
3.720
GLY229
3.486
ALA230
3.661
|
|||||
| PDB ID: 1NZW Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NADH and Mg2+ | ||||||
| Method | X-ray diffraction | Resolution | 2.65 Å | Mutation | Yes | [1] |
| PDB Sequence |
AVPAPNQQPE
16 VFCNQIFINN26 EWHDAVSRKT36 FPTVNPSTGE46 VICQVAEGDK56 EDVDKAVKAA 66 RAAFQLGSPW76 RRMDASHRGR86 LLNRLADLIE96 RDRTYLAALE106 TLDNGKPYVI 116 SYLVDLDMVL126 KCLRYYAGWA136 DKYHGKTIPI146 DGDFFSYTRH156 EPVGVCGQII 166 PWNFPLLMQA176 WKLGPALATG186 NVVVMKVAEQ196 TPLTALYVAN206 LIKEAGFPPG 216 VVNIVPGFGP226 TAGAAIASHE236 DVDKVAFTGS246 TEIGRVIQVA256 AGSSNLKRVT 266 LELGGKSPNI276 IMSDADMDWA286 VEQAHFALFF296 NQGQCSCAGS306 RTFVQEDIYD 316 EFVERSVARA326 KSRVVGNPFD336 SKTEQGPQVD346 ETQFKKILGY356 INTGKQEGAK 366 LLCGGGIAAD376 RGYFIQPTVF386 GDVQDGMTIA396 KEEIFGPVMQ406 ILKFKTIEEV 416 VGRANNSTYG426 LAAAVFTKDL436 DKANYLSQAL446 QAGTVWVNCY456 DVFGAQSPFG 466 GYKMSGSGRE476 LGEYGLQAYT486 EVKTVTVKVP496 QKNS
|
|||||
|
|
ILE165
3.434
ILE166
3.096
PRO167
3.355
TRP168
2.989
ASN169
3.149
LYS192
2.859
VAL193
4.133
ALA194
3.761
GLU195
2.629
GLN196
3.963
GLY223
4.607
PHE224
4.051
GLY225
3.290
PRO226
3.709
GLY229
3.302
ALA230
3.281
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase. Biochemistry. 2003 Jun 17;42(23):7100-9. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.