Binding Site Information of Target

Content Navigation (  All   None )                                      
Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T59445 Target Info
Target Name Sorbitoldehydrogenase (SORD)
Synonyms SORD; SDH; L-iditol2-dehydrogenase
Target Type Literature-reported Target
Gene Name SORD
Biochemical Class Short-chain dehydrogenases reductase
UniProt ID
DHSO_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Nicotinamide-Adenine-Dinucleotide Ligand Info
Structure Description human SDH/NAD+ complex PDB:1PL8
Method X-ray diffraction Resolution 1.90 Å Mutation No [1]
PDB Sequence
AAAAKPNNLS
10
LVVHGPGDLR
20
LENYPIPEPG
30
PNEVLLRMHS
40
VGICGSDVHY
50

WEYGRIGNFI
60
VKKPMVLGHE
70
ASGTVEKVGS
80
SVKHLKPGDR
90
VAIEPGAPRE
100

NDEFCKMGRY
110
NLSPSIFFCA
120
TPPDDGNLCR
130
FYKHNAAFCY
140
KLPDNVTFEE
150

GALIEPLSVG
160
IHACRRGGVT
170
LGHKVLVCGA
180
GPIGMVTLLV
190
AKAMGAAQVV
200

VTDLSATRLS
210
KAKEIGADLV
220
LQISKESPQE
230
IARKVEGQLG
240
CKPEVTIECT
250

GAEASIQAGI
260
YATRSGGTLV
270
LVGLGSEMTT
280
VPLLHAAIRE
290
VDIKGVFRYC
300

NTWPVAISML
310
ASKSVNVKPL
320
VTHRFPLEKA
330
LEAFETFKKG
340
LGLKIMLKCD
350

PSDQNP
Residue
Distance (Å)
VAL159
4.070
CYS178
4.961
GLY179
3.907
ALA180
4.066
GLY181
3.274
PRO182
3.283
ILE183
3.018
GLY184
4.174
THR202
3.842
ASP203
2.505
LEU204
3.676
SER205
4.419
ARG208
2.805
Residue
Distance (Å)
ILE223
3.841
CYS249
3.124
THR250
3.361
GLY251
4.697
ALA252
3.809
ALA254
4.759
SER255
4.107
VAL272
3.077
GLY273
3.456
LEU274
2.935
VAL296
2.828
PHE297
3.609
ARG298
2.565
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 4-[2-(Hydroxymethyl)pyrimidin-4-YL]-N,N-dimethylpiperazine-1-sulfonamide Ligand Info
Structure Description Human SDH/NADH/inhibitor complex PDB:1PL6
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [1]
PDB Sequence
AAAAKPNNLS
10
LVVHGPGDLR
20
LENYPIPEPG
30
PNEVLLRHSV
41
GICGSDVHYW
51

EYGRIGNFIV
61
KKPVLGHEAS
72
GTVEKVGSSV
82
KHLKPGDRVA
92
IEPGAPREND
102

EFCKGRYNLS
113
PSIFFCATPP
123
DDGNLCRFYK
133
HNAAFCYKLP
143
DNVTFEEGAL
153

IEPLSVGIHA
163
CRRGGVTLGH
173
KVLVCGAGPI
183
GVTLLVAKAG
195
AAQVVVTDLS
205

ATRLSKAKEI
215
GADLVLQISK
225
ESPQEIARKV
235
EGQLGCKPEV
245
TIECTGAEAS
255

IQAGIYATRS
265
GGTLVLVGLG
275
SETTVPLLHA
286
AIREVDIKGV
296
FRYCNTWPVA
306

ISLASKSVNV
317
KPLVTHRFPL
327
EKALEAFETF
337
KKGLGLKILK
348
CDPSDQNP
Residue
Distance (Å)
CYS44
3.373
SER46
3.337
TYR50
3.516
ILE56
3.535
PHE59
3.396
HIS69
3.009
PHE118
3.951
Residue
Distance (Å)
THR121
3.600
GLU155
2.389
VAL159
4.920
LEU274
3.506
PHE297
3.394
ARG298
3.917
TYR299
4.360
Ligand Name: Selenomethionine Ligand Info
Structure Description Human SDH/NADH/inhibitor complex PDB:1PL6
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [1]
PDB Sequence
AAAAKPNNLS
10
LVVHGPGDLR
20
LENYPIPEPG
30
PNEVLLRHSV
41
GICGSDVHYW
51

EYGRIGNFIV
61
KKPVLGHEAS
72
GTVEKVGSSV
82
KHLKPGDRVA
92
IEPGAPREND
102

EFCKGRYNLS
113
PSIFFCATPP
123
DDGNLCRFYK
133
HNAAFCYKLP
143
DNVTFEEGAL
153

IEPLSVGIHA
163
CRRGGVTLGH
173
KVLVCGAGPI
183
GVTLLVAKAG
195
AAQVVVTDLS
205

ATRLSKAKEI
215
GADLVLQISK
225
ESPQEIARKV
235
EGQLGCKPEV
245
TIECTGAEAS
255

IQAGIYATRS
265
GGTLVLVGLG
275
SETTVPLLHA
286
AIREVDIKGV
296
FRYCNTWPVA
306

ISLASKSVNV
317
KPLVTHRFPL
327
EKALEAFETF
337
KKGLGLKILK
348
CDPSDQNP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MSE or .MSE2 or .MSE3 or :3MSE;style chemicals stick;color identity;select .A:11 or .A:12 or .A:13 or .A:36 or .A:37 or .A:39 or .A:40 or .A:41 or .A:42 or .A:50 or .A:61 or .A:63 or .A:64 or .A:66 or .A:67 or .A:72 or .A:73 or .A:74 or .A:93 or .A:103 or .A:104 or .A:105 or .A:106 or .A:108 or .A:109 or .A:120 or .A:121 or .A:122 or .A:124 or .A:125 or .A:126 or .A:127 or .A:129 or .A:130 or .A:131 or .A:132 or .A:149 or .A:152 or .A:153 or .A:164 or .A:165 or .A:169 or .A:170 or .A:171 or .A:179 or .A:180 or .A:181 or .A:182 or .A:183 or .A:184 or .A:186 or .A:187 or .A:188 or .A:189 or .A:190 or .A:191 or .A:192 or .A:193 or .A:195 or .A:196 or .A:201 or .A:208 or .A:211 or .A:212 or .A:215 or .A:253 or .A:276 or .A:277 or .A:279 or .A:280 or .A:305 or .A:306 or .A:307 or .A:308 or .A:310 or .A:311 or .A:312 or .A:313 or .A:314 or .A:315 or .A:320 or .A:321 or .A:323 or .A:324 or .A:325 or .A:343 or .A:344 or .A:345 or .A:347 or .A:348 or .A:349 or .A:350; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU11
4.060
VAL12
3.441
VAL13
2.915
LEU36
3.072
ARG37
1.328
HIS39
1.331
SER40
4.236
VAL41
3.631
GLY42
3.743
TYR50
3.931
VAL61
4.145
LYS63
3.260
PRO64
1.329
VAL66
1.328
LEU67
3.521
SER72
3.896
GLY73
3.508
THR74
4.478
ILE93
3.675
GLU103
2.966
PHE104
3.240
CYS105
3.210
LYS106
1.334
GLY108
1.337
ARG109
3.504
ALA120
3.273
THR121
3.780
PRO122
3.253
ASP124
3.788
ASP125
3.299
GLY126
4.820
ASN127
3.657
CYS129
3.042
ARG130
2.756
PHE131
4.400
TYR132
3.774
GLU149
3.607
ALA152
3.863
LEU153
3.470
CYS164
3.621
ARG165
4.818
VAL169
3.363
THR170
3.946
LEU171
3.758
GLY179
4.629
ALA180
3.615
Residue
Distance (Å)
GLY181
2.913
PRO182
3.321
ILE183
3.135
GLY184
1.329
VAL186
1.331
THR187
3.144
LEU188
3.223
LEU189
2.978
VAL190
2.922
ALA191
3.243
LYS192
3.124
ALA193
1.334
GLY195
1.326
ALA196
3.706
VAL201
3.949
ARG208
4.525
LYS211
4.618
ALA212
3.462
ILE215
3.726
GLU253
4.699
SER276
3.260
GLU277
1.328
THR279
1.329
THR280
4.522
VAL305
2.946
ALA306
3.167
ILE307
3.287
SER308
1.333
LEU310
1.331
ALA311
3.407
SER312
3.267
LYS313
3.210
SER314
2.820
VAL315
3.717
LEU320
4.088
VAL321
3.959
HIS323
2.958
ARG324
3.156
PHE325
2.827
LEU343
4.603
LYS344
3.905
ILE345
1.329
LEU347
1.328
LYS348
4.125
CYS349
3.678
ASP350
3.412
References  Top
REF 1 X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase. Structure. 2003 Sep;11(9):1071-85.

If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.