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 | 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: 1O04 Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ | ||||||
| Method | X-ray diffraction | Resolution | 1.42 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
3.206
ILE166
2.832
PRO167
3.345
TRP168
2.853
ASN169
3.235
MET174
3.886
TRP177
3.883
LYS192
2.732
VAL193
4.018
ALA194
3.731
GLU195
2.667
GLN196
4.846
GLY223
4.643
PHE224
4.026
GLY225
3.342
PRO226
3.796
GLY229
3.231
ALA230
3.286
PHE243
3.133
|
|||||
| PDB ID: 2ONP Arg475Gln Mutant of Human Mitochondrial Aldehyde Dehydrogenase, complexed with NAD+ | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | Yes | [2] |
| 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 GYKMSGSGQE476 LGEYGLQAYT486 EVKTVTVKVP496 QKNS
|
|||||
|
|
ILE165
3.343
ILE166
2.916
PRO167
3.233
TRP168
3.006
ASN169
3.095
LYS192
2.906
VAL193
4.080
ALA194
3.787
GLU195
2.723
GLN196
3.806
GLY223
4.625
PHE224
4.103
GLY225
3.257
PRO226
3.848
GLY229
3.338
ALA230
3.428
|
|||||
| PDB ID: 1O01 Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(H) and Mg2+ | ||||||
| Method | X-ray diffraction | Resolution | 2.15 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
3.352
ILE166
2.866
PRO167
3.250
TRP168
2.759
ASN169
3.204
LYS192
2.837
VAL193
4.123
ALA194
3.680
GLU195
2.779
GLN196
3.750
GLY223
4.673
PHE224
4.149
GLY225
3.333
PRO226
3.794
GLY229
3.271
ALA230
3.385
|
|||||
| PDB ID: 4FR8 Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [3] |
| PDB Sequence |
VPAPNQQPEV
17 FCNQIFINNE27 WHDAVSRKTF37 PTVNPSTGEV47 ICQVAEGDKE57 DVDKAVKAAR 67 AAFQLGSPWR77 RMDASHRGRL87 LNRLADLIER97 DRTYLAALET107 LDNGKPYVIS 117 YLVDLDMVLK127 CLRYYAGWAD137 KYHGKTIPID147 GDFFSYTRHE157 PVGVCGQIIP 167 WNFPLLMQAW177 KLGPALATGN187 VVVMKVAEQT197 PLTALYVANL207 IKEAGFPPGV 217 VNIVPGFGPT227 AGAAIASHED237 VDKVAFTGST247 EIGRVIQVAA257 GSSNLKRVTL 267 QLGGKSPNII277 MSDADMDWAV287 EQAHFALFFN297 QGQSCSAGSR307 TFVQEDIYDE 317 FVERSVARAK327 SRVVGNPFDS337 KTEQGPQVDE347 TQFKKILGYI357 NTGKQEGAKL 367 LCGGGIAADR377 GYFIQPTVFG387 DVQDGMTIAK397 EEIFGPVMQI407 LKFKTIEEVV 417 GRANNSTYGL427 AAAVFTKDLD437 KANYLSQALQ447 AGTVWVNCYD457 VFGAQSPFGG 467 YKMSGSGREL477 GEYGLQAYTE487 VKTVTVKVPQ497 KNS
|
|||||
|
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:165 or .A:166 or .A:167 or .A:168 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196 or .A:223 or .A:224 or .A:225 or .A:226 or .A:229 or .A:230 or .A:243 or .A:244 or .A:245 or .A:246 or .A:249 or .A:252 or .A:253 or .A:349 or .A:352 or .A:399 or .A:400 or .A:401; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE165
3.311
ILE166
2.704
PRO167
4.532
TRP168
2.830
LYS192
2.487
VAL193
4.105
ALA194
3.586
GLU195
3.048
GLN196
3.233
GLY223
4.572
PHE224
4.061
GLY225
3.273
PRO226
3.786
GLY229
3.320
|
|||||
| PDB ID: 3N82 T244A mutant of Human mitochondrial aldehyde dehydrogenase, NADH complex | ||||||
| Method | X-ray diffraction | Resolution | 2.25 Å | Mutation | Yes | [4] |
| 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 DVDKVAFAGS246 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
|
|||||
|
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:165 or .A:166 or .A:167 or .A:168 or .A:169 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196 or .A:223 or .A:224 or .A:225 or .A:226 or .A:229 or .A:230 or .A:243 or .A:244 or .A:245 or .A:246 or .A:249 or .A:252 or .A:253 or .A:268 or .A:269 or .A:270 or .A:302 or .A:349 or .A:352 or .A:399 or .A:400 or .A:401; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE165
3.368
ILE166
2.734
PRO167
3.338
TRP168
2.826
ASN169
3.597
LYS192
2.656
VAL193
4.076
ALA194
3.575
GLU195
2.677
GLN196
3.702
GLY223
4.513
PHE224
4.147
GLY225
3.241
PRO226
3.744
GLY229
3.277
ALA230
3.382
|
|||||
| PDB ID: 4FQF Crystal structure of a thionitrate intermediate of human aldehyde dehydrogenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.28 Å | Mutation | No | [3] |
| PDB Sequence |
QQPEVFCNQI
22 FINNEWHDAV32 SRKTFPTVNP42 STGEVICQVA52 EGDKEDVDKA62 VKAARAAFQL 72 GSPWRRMDAS82 HRGRLLNRLA92 DLIERDRTYL102 AALETLDNGK112 PYVISYLVDL 122 DMVLKCLRYY132 AGWADKYHGK142 TIPIDGDFFS152 YTRHEPVGVC162 GQIIPWNFPL 172 LMQAWKLGPA182 LATGNVVVMK192 VAEQTPLTAL202 YVANLIKEAG212 FPPGVVNIVP 222 GFGPTAGAAI232 ASHEDVDKVA242 FTGSTEIGRV252 IQVAAGSSNL262 KRVTLELGGK 272 SPNIIMSDAD282 MDWAVEQAHF292 ALFFNQGQCC302 CAGSRTFVQE312 DIYDEFVERS 322 VARAKSRVVG332 NPFDSKTEQG342 PQVDETQFKK352 ILGYINTGKQ362 EGAKLLCGGG 372 IAADRGYFIQ382 PTVFGDVQDG392 MTIAKEEIFG402 PVMQILKFKT412 IEEVVGRANN 422 STYGLAAAVF432 TKDLDKANYL442 SQALQAGTVW452 VNCYDVFGAQ462 SPFGGYKMSG 472 SGRELGEYGL482 QAYTEVKTVT492 VKVPQKNS
|
|||||
|
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:165 or .A:166 or .A:167 or .A:168 or .A:169 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196 or .A:223 or .A:224 or .A:225 or .A:226 or .A:229 or .A:230 or .A:243 or .A:244 or .A:245 or .A:246 or .A:249 or .A:252 or .A:253 or .A:268 or .A:269 or .A:270 or .A:302 or .A:349 or .A:352 or .A:399 or .A:401; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE165
3.319
ILE166
2.896
PRO167
3.307
TRP168
2.915
ASN169
3.615
LYS192
2.547
VAL193
4.178
ALA194
3.566
GLU195
2.805
GLN196
3.768
GLY223
4.700
PHE224
3.842
GLY225
3.231
PRO226
3.834
GLY229
3.396
ALA230
3.337
|
|||||
| PDB ID: 1NZX Human mitochondrial aldehyde dehydrogenase complexed with NAD+ 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
|
|||||
|
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:165 or .A:166 or .A:167 or .A:168 or .A:192 or .A:193 or .A:194 or .A:195 or .A:223 or .A:224 or .A:225 or .A:226 or .A:229 or .A:230 or .A:243 or .A:244 or .A:245 or .A:246 or .A:249 or .A:252 or .A:253 or .A:349 or .A:401; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE165
3.294
ILE166
3.028
PRO167
3.880
TRP168
2.905
LYS192
2.754
VAL193
4.103
ALA194
3.948
GLU195
4.063
GLY223
4.795
PHE224
4.194
GLY225
3.314
PRO226
4.111
|
|||||
| PDB ID: 1O00 Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ showing dual NAD(H) conformations | ||||||
| Method | X-ray diffraction | Resolution | 2.60 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
|
|||||
|
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:165 or .A:166 or .A:167 or .A:168 or .A:169 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196 or .A:223 or .A:224 or .A:225 or .A:226 or .A:229 or .A:230 or .A:243 or .A:244 or .A:245 or .A:246 or .A:249 or .A:252 or .A:253 or .A:268 or .A:269 or .A:270 or .A:302 or .A:349 or .A:352 or .A:399 or .A:401; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE165
3.319
ILE166
2.811
PRO167
3.233
TRP168
3.368
ASN169
3.739
LYS192
2.922
VAL193
4.031
ALA194
3.544
GLU195
2.725
GLN196
3.820
GLY223
4.690
PHE224
4.234
GLY225
3.377
PRO226
3.823
GLY229
3.266
ALA230
3.467
|
|||||
| PDB ID: 1CW3 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ | ||||||
| Method | X-ray diffraction | Resolution | 2.58 Å | Mutation | No | [5] |
| 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
|
|||||
|
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:165 or .A:166 or .A:167 or .A:168 or .A:169 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196 or .A:223 or .A:224 or .A:225 or .A:226 or .A:229 or .A:230 or .A:243 or .A:244 or .A:245 or .A:246 or .A:249 or .A:252 or .A:253 or .A:268 or .A:269 or .A:270 or .A:302 or .A:349 or .A:352 or .A:399 or .A:401; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE165
3.303
ILE166
2.685
PRO167
3.481
TRP168
2.491
ASN169
3.733
LYS192
2.649
VAL193
4.127
ALA194
3.819
GLU195
2.898
GLN196
3.829
GLY223
4.606
PHE224
4.234
GLY225
3.251
PRO226
3.926
GLY229
3.397
ALA230
3.375
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase. Biochemistry. 2003 Jun 17;42(23):7100-9. | ||||
| REF 2 | Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487. J Biol Chem. 2007 Apr 27;282(17):12940-50. | ||||
| REF 3 | Vascular bioactivation of nitroglycerin by aldehyde dehydrogenase-2: reaction intermediates revealed by crystallography and mass spectrometry. J Biol Chem. 2012 Nov 2;287(45):38124-34. | ||||
| REF 4 | Conformational Selection During Catalysis: The role of Threonine 244 in ALDH2 | ||||
| REF 5 | Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. | ||||
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