Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T15053 Target Info
Target Name Lactate dehydrogenase A (LDHA)
Synonyms Renal carcinoma antigen NYREN59; Renal carcinoma antigen NY-REN-59; PIG19; Llactate dehydrogenase A chain; LDHM; LDH-M; LDH-A; LDH muscle subunit; L-lactate dehydrogenase A chain; Cell proliferationinducing gene 19 protein; Cell proliferation-inducing gene 19 protein
Target Type Literature-reported Target
Gene Name LDHA
Biochemical Class CH-OH donor oxidoreductase
UniProt ID
LDHA_HUMAN
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: 5W8K      Crystal Structure of Lactate Dehydrogenase A in complex with inhibitor compound 29 and NADH
Method X-ray diffraction Resolution 1.60 Å Mutation No [1]
PDB Sequence
ATLKDQLIYN
10
LLKEQTPQNK
21
ITVVGVGAVG
31
MACAISILMK
41
DLADELALVD
51

VIEDKLKGEM
61
MDLQHGSLFL
71
RTPKIVSGKD
81
YNVTANSKLV
91
IITAGARLNL
108

VQRNVNIFKF
118
IIPNVVKYSP
128
NCKLLIVSNP
138
VDILTYVAWK
148
ISGFPKNRVI
158

GSGCNLDSAR
168
FRYLMGERLG
178
VHPLSCHGWV
188
LGEHGDSSVP
198
VWSGMNVAGV
208

SLKTLHPDLG
218
TDKDKEQWKE
228
VHKQVVESAY
238
EVIKLKGYTS
248
WAIGLSVADL
258

AESIMKNLRR
268
VHPVSTMIKG
278
LYGIKDDVFL
288
SVPCILGQNG
298
ISDLVKVTLT
308

SEEEARLKKS
318
ADTLWGIQKE
328
LQF
Residue
Distance (Å)
VAL25
3.803
GLY26
3.927
VAL27
4.110
GLY28
3.247
ALA29
3.234
VAL30
2.956
GLY31
4.299
VAL50
4.515
ASP51
2.708
VAL52
3.452
ILE53
3.311
LYS56
2.810
TYR82
4.195
THR94
3.119
ALA95
3.321
GLY96
3.276
ALA97
2.999
Residue
Distance (Å)
ARG98
2.913
ASN112
4.149
ILE115
3.635
PHE118
4.494
ILE119
3.727
VAL135
2.988
SER136
3.629
ASN137
3.003
VAL139
3.954
SER160
3.109
GLY161
4.571
LEU164
3.692
HIS192
3.193
TYR246
4.294
THR247
3.463
ILE251
3.620
PDB ID: 5W8L      Crystal Structure of Lactate Dehydrogenase A in complex with inhibitor compound 59 and NADH
Method X-ray diffraction Resolution 1.95 Å Mutation No [1]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Residue
Distance (Å)
VAL25
3.830
GLY26
3.725
VAL27
3.912
GLY28
3.356
ALA29
3.194
VAL30
3.009
GLY31
4.346
VAL50
4.589
ASP51
2.643
VAL52
3.385
ILE53
3.388
TYR82
4.341
THR94
3.205
ALA95
3.167
GLY96
3.209
ALA97
4.636
Residue
Distance (Å)
ARG98
2.980
ASN112
4.752
ILE115
3.569
PHE118
3.933
ILE119
3.674
VAL135
3.003
SER136
3.505
ASN137
2.887
VAL139
3.910
SER160
2.935
GLY161
4.396
LEU164
3.626
HIS192
3.162
TYR246
4.256
THR247
3.239
ILE251
3.507
PDB ID: 6MV8      LDHA structure in complex with inhibitor 14
Method X-ray diffraction Resolution 1.95 Å Mutation No [2]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGALNL
108

VQRNVNIFKF
118
IIPNVVKYSP
128
NCKLLIVSNP
138
VDILTYVAWK
148
ISGFPKNRVI
158

GSGCNLDSAR
168
FRYLMGERLG
178
VHPLSCHGWV
188
LGEHGDSSVP
198
VWSGMNVAGV
208

SLKTLHPDLG
218
TDKDKEQWKE
228
VHKQVVESAY
238
EVIKLKGYTS
248
WAIGLSVADL
258

AESIMKNLRR
268
VHPVSTMIKG
278
LYGIKDDVFL
288
SVPCILGQNG
298
ISDLVKVTLT
308

SEEEARLKKS
318
ADTLWGIQKE
328
LQF
Residue
Distance (Å)
VAL25
3.842
GLY26
4.148
VAL27
4.038
GLY28
3.361
ALA29
3.245
VAL30
3.011
GLY31
4.311
VAL50
4.547
ASP51
2.555
VAL52
3.690
ILE53
3.366
TYR82
4.254
THR94
3.143
ALA95
3.380
GLY96
3.505
Residue
Distance (Å)
ASN112
4.982
ILE115
3.477
PHE118
4.614
ILE119
3.662
VAL135
3.078
SER136
3.646
ASN137
2.887
VAL139
3.876
SER160
4.211
GLY161
4.554
LEU164
3.772
HIS192
3.175
TYR246
4.339
THR247
3.414
ILE251
3.616
PDB ID: 6Q13      CRYSTAL STRUCTURE OF LDHA IN COMPLEX WITH COMPOUND NCGC00420737-09 AT 2.00 A RESOLUTION
Method X-ray diffraction Resolution 2.00 Å Mutation No [3]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.805
GLY26
3.851
VAL27
3.976
GLY28
3.338
ALA29
3.202
VAL30
2.988
GLY31
4.317
VAL50
4.513
ASP51
2.722
VAL52
3.428
ILE53
3.403
TYR82
4.329
THR94
3.156
ALA95
3.158
GLY96
3.104
ALA97
4.554
Residue
Distance (Å)
ARG98
2.960
ASN112
4.559
ILE115
3.600
PHE118
3.754
ILE119
3.638
VAL135
2.968
SER136
3.632
ASN137
2.954
VAL139
3.845
SER160
3.742
GLY161
4.589
LEU164
3.937
HIS192
3.444
TYR246
4.328
THR247
3.351
ILE251
3.421
PDB ID: 6MVA      LDHA structure in complex with inhibitor 14
Method X-ray diffraction Resolution 2.02 Å Mutation No [4]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGAEGE
103

SRLNLVQRNV
113
NIFKFIIPNV
123
VKYSPNCKLL
133
IVSNPVDILT
143
YVAWKISGFP
153

KNRVIGSGCN
163
LDSARFRYLM
173
GERLGVHPLS
183
CHGWVLGEHG
193
DSSVPVWSGM
203

NVAGVSLKTL
213
HPDLGTDKDK
223
EQWKEVHKQV
233
VESAYEVIKL
243
KGYTSWAIGL
253

SVADLAESIM
263
KNLRRVHPVS
273
TMIKGLYGIK
283
DDVFLSVPCI
293
LGQNGISDLV
303

KVTLTSEEEA
313
RLKKSADTLW
323
GIQKELQF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.819
GLY26
3.851
VAL27
4.086
GLY28
3.438
ALA29
3.336
VAL30
3.146
GLY31
4.383
VAL50
4.517
ASP51
2.703
VAL52
3.571
ILE53
3.292
TYR82
4.080
THR94
3.155
ALA95
3.324
GLY96
3.601
Residue
Distance (Å)
ILE115
3.527
PHE118
4.360
ILE119
3.633
VAL135
3.073
SER136
3.713
ASN137
2.814
VAL139
3.952
SER160
4.123
GLY161
4.412
LEU164
3.922
HIS192
3.400
TYR246
4.437
THR247
3.589
ILE251
3.402
PDB ID: 6Q0D      CRYSTAL STRUCTURE OF LDHA IN COMPLEX WITH COMPOUND NCGC00384414-01 AT 2.05 A RESOLUTION
Method X-ray diffraction Resolution 2.05 Å Mutation No [3]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:56 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.963
GLY26
3.818
VAL27
4.150
GLY28
3.298
ALA29
3.029
VAL30
2.940
GLY31
4.398
VAL50
4.666
ASP51
2.693
VAL52
3.457
ILE53
3.541
LYS56
4.793
TYR82
4.370
THR94
3.192
ALA95
3.217
GLY96
3.347
ALA97
4.782
Residue
Distance (Å)
ARG98
2.630
ASN112
4.608
ILE115
3.557
PHE118
3.915
ILE119
3.680
VAL135
2.999
SER136
3.588
ASN137
3.052
VAL139
3.849
SER160
3.925
GLY161
4.367
LEU164
3.774
HIS192
3.238
TYR246
4.215
THR247
3.247
ILE251
3.668
PDB ID: 6SBU      X-ray Structure of Human LDHA with an Allosteric Inhibitor (Compound 3)
Method X-ray diffraction Resolution 2.91 Å Mutation No [5]
PDB Sequence
ATLKDQLIYN
11
LLKTPQNKIT
24
VVGVGAVGMA
34
CAISILMKDL
44
ADELALVDVI
54

EDKLKGEMMD
64
LQHGSLFLRT
74
PKIVSGKDYN
84
VTANSKLVII
94
TAGARQQEGE
104

SRLNLVQRNV
114
NIFKFIIPNV
124
VKYSPNCKLL
134
IVSNPVDILT
144
YVAWKISGFP
154

KNRVIGSGCN
164
LDSARFRYLM
174
GERLGVHPLS
184
CHGWVLGEHG
194
DSSVPVWSGM
204

NVAGVSLKTL
214
HPDLGTDKDK
224
EQWKEVHKQV
234
VESAYEVIKL
244
KGYTSWAIGL
254

SVADLAESIM
264
KNLRRVHPVS
274
TMIKGLYGIK
284
DDVFLSVPCI
294
LGQNGISDLV
304

KVTLTSEEEA
314
RLKKSADTLW
324
GIQKELQF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:51 or .A:52 or .A:53 or .A:54 or .A:83 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:113 or .A:116 or .A:119 or .A:120 or .A:136 or .A:137 or .A:138 or .A:139 or .A:140 or .A:161 or .A:193 or .A:248 or .A:252; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL26
4.070
GLY27
4.165
VAL28
4.412
GLY29
3.389
ALA30
3.791
VAL31
2.957
GLY32
3.909
VAL51
4.454
ASP52
2.668
VAL53
3.442
ILE54
3.178
TYR83
3.424
THR95
2.691
ALA96
3.148
GLY97
3.154
Residue
Distance (Å)
ALA98
4.426
ARG99
3.136
ASN113
4.539
ILE116
3.797
PHE119
3.512
ILE120
3.702
VAL136
3.221
SER137
3.367
ASN138
2.361
PRO139
4.915
VAL140
4.936
SER161
3.634
HIS193
3.406
THR248
3.745
ILE252
3.208
PDB ID: 4JNK      Lactate Dehydrogenase A in complex with inhibitor compound 22
Method X-ray diffraction Resolution 1.90 Å Mutation No [6]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARSR
105

LNLVQRNVNI
115
FKFIIPNVVK
125
YSPNCKLLIV
135
SNPVDILTYV
145
AWKISGFPKN
155

RVIGSGCNLD
165
SARFRYLMGE
175
RLGVHPLSCH
185
GWVLGEHGDS
195
SVPVWSGMNV
205

AGVSLKTLHP
215
DLGTDKDKEQ
225
WKEVHKQVVE
235
SAYEVIKLKG
245
YTSWAIGLSV
255

ADLAESIMKN
265
LRRVHPVSTM
275
IKGLYGIKDD
285
VFLSVPCILG
295
QNGISDLVKV
305

TLTSEEEARL
315
KKSADTLWGI
325
QKELQF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.954
GLY26
4.081
VAL27
4.266
GLY28
3.230
ALA29
3.203
VAL30
2.917
GLY31
4.338
VAL50
4.631
ASP51
2.849
VAL52
3.484
ILE53
3.357
TYR82
4.241
THR94
3.191
ALA95
3.447
GLY96
3.349
ALA97
3.058
Residue
Distance (Å)
ARG98
2.789
ASN112
4.436
ILE115
3.766
PHE118
4.528
ILE119
3.604
VAL135
2.957
SER136
3.657
ASN137
3.005
VAL139
3.925
SER160
3.263
GLY161
4.711
LEU164
3.700
HIS192
3.143
TYR246
4.282
THR247
3.272
ILE251
3.439
PDB ID: 4RLS      Lactate Dehydrogenase in complex with inhibitor compound 47
Method X-ray diffraction Resolution 1.91 Å Mutation No [7]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
4.030
GLY26
4.169
VAL27
4.061
GLY28
3.182
ALA29
3.210
VAL30
2.987
GLY31
4.217
VAL50
4.447
ASP51
2.718
VAL52
3.567
ILE53
3.590
TYR82
3.975
THR94
2.732
ALA95
3.322
GLY96
3.701
ALA97
4.897
Residue
Distance (Å)
ARG98
3.279
ILE115
3.334
PHE118
3.941
ILE119
3.630
VAL135
3.008
SER136
3.748
ASN137
2.734
VAL139
3.966
SER160
3.545
GLY161
4.814
LEU164
4.580
HIS192
3.621
TYR246
4.561
THR247
3.779
ILE251
3.255
PDB ID: 4QO8      Lactate Dehydrogenase A in complex with substituted 3-Hydroxy-2-mercaptocyclohex-2-enone compound 104
Method X-ray diffraction Resolution 2.00 Å Mutation No [8]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:98 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.982
GLY26
3.957
VAL27
4.163
GLY28
3.399
ALA29
3.371
VAL30
3.009
GLY31
4.319
VAL50
4.559
ASP51
2.727
VAL52
3.325
ILE53
3.357
TYR82
4.192
THR94
3.184
ALA95
3.488
GLY96
3.629
ARG98
3.178
Residue
Distance (Å)
ASN112
4.769
ILE115
3.569
PHE118
4.611
ILE119
3.621
VAL135
3.133
SER136
3.571
ASN137
2.908
VAL139
3.874
SER160
3.196
GLY161
4.344
LEU164
3.923
HIS192
3.194
TYR246
4.370
THR247
3.518
ILE251
3.557
PDB ID: 4M49      Lactate Dehydrogenase A in complex with a substituted pyrazine inhibitor compound 18
Method X-ray diffraction Resolution 2.05 Å Mutation No [9]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
4.051
GLY26
4.144
VAL27
4.279
GLY28
3.274
ALA29
3.213
VAL30
3.026
GLY31
4.271
VAL50
4.456
ASP51
2.686
VAL52
3.416
ILE53
3.575
TYR82
3.964
THR94
3.248
ALA95
3.498
GLY96
3.735
Residue
Distance (Å)
ILE115
3.729
PHE118
4.339
ILE119
3.763
VAL135
3.072
SER136
3.534
ASN137
2.857
VAL139
4.006
SER160
3.010
GLY161
4.619
LEU164
4.033
HIS192
3.520
TYR246
4.552
THR247
3.551
ILE251
3.568
PDB ID: 4R68      Lactate Dehydrogenase in complex with inhibitor compound 31
Method X-ray diffraction Resolution 2.11 Å Mutation No [10]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:98 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.951
GLY26
3.910
VAL27
4.344
GLY28
3.417
ALA29
3.360
VAL30
3.107
GLY31
4.317
VAL50
4.536
ASP51
2.734
VAL52
3.542
ILE53
3.542
TYR82
4.097
THR94
3.278
ALA95
3.283
GLY96
3.310
ARG98
2.554
Residue
Distance (Å)
ASN112
4.728
ILE115
3.483
PHE118
4.167
ILE119
3.703
VAL135
3.002
SER136
3.838
ASN137
2.910
VAL139
3.776
SER160
3.970
GLY161
4.364
LEU164
3.832
HIS192
3.147
TYR246
4.523
THR247
3.361
ILE251
3.725
PDB ID: 4QO7      Lactate Dehydrogenase A in complex with substituted 3-Hydroxy-2-mercaptocyclohex-2-enone compound 7
Method X-ray diffraction Resolution 2.14 Å Mutation No [8]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.751
GLY26
3.975
VAL27
4.137
GLY28
3.451
ALA29
3.231
VAL30
2.940
GLY31
4.304
VAL50
4.496
ASP51
2.744
VAL52
3.482
ILE53
3.583
TYR82
4.111
THR94
3.379
ALA95
3.452
GLY96
3.425
ALA97
3.807
Residue
Distance (Å)
ARG98
2.800
ASN112
4.870
ILE115
3.664
PHE118
4.652
ILE119
3.635
VAL135
3.049
SER136
3.746
ASN137
2.800
VAL139
3.967
SER160
4.153
GLY161
4.530
LEU164
3.797
HIS192
3.022
TYR246
4.381
THR247
3.390
ILE251
3.458
PDB ID: 1I10      HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE
Method X-ray diffraction Resolution 2.30 Å Mutation No [11]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:56 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:108 or .A:112 or .A:115 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
4.022
GLY26
4.150
VAL27
3.857
GLY28
3.033
ALA29
2.876
VAL30
2.714
GLY31
4.217
VAL50
4.656
ASP51
2.457
VAL52
3.551
ILE53
3.696
LYS56
3.332
TYR82
4.233
THR94
3.084
ALA95
3.396
GLY96
3.332
ALA97
2.681
Residue
Distance (Å)
ARG98
2.983
GLN99
4.238
LEU108
3.859
ASN112
3.914
ILE115
3.756
ILE119
3.666
VAL135
2.855
SER136
3.763
ASN137
2.892
VAL139
3.863
SER160
3.150
GLY161
4.708
LEU164
3.609
HIS192
3.094
TYR246
4.317
THR247
3.283
ILE251
3.437
PDB ID: 4R69      Lactate Dehydrogenase in complex with inhibitor compound 13
Method X-ray diffraction Resolution 3.19 Å Mutation No [10]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQL
106

NLVQRNVNIF
116
KFIIPNVVKY
126
SPNCKLLIVS
136
NPVDILTYVA
146
WKISGFPKNR
156

VIGSGCNLDS
166
ARFRYLMGER
176
LGVHPLSCHG
186
WVLGEHGDSS
196
VPVWSGMNVA
206

GVSLKTLHPD
216
LGTDKDKEQW
226
KEVHKQVVES
236
AYEVIKLKGY
246
TSWAIGLSVA
256

DLAESIMKNL
266
RRVHPVSTMI
276
KGLYGIKDDV
286
FLSVPCILGQ
296
NGISDLVKVT
306

LTSEEEARLK
316
KSADTLWGIQ
326
KELQF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:56 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:108 or .A:112 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:165 or .A:192 or .A:246 or .A:247 or .A:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.829
GLY26
3.611
VAL27
3.975
GLY28
3.287
ALA29
3.109
VAL30
3.051
GLY31
4.256
VAL50
4.109
ASP51
2.722
VAL52
3.484
ILE53
3.219
LYS56
4.631
TYR82
3.777
THR94
3.385
ALA95
3.365
GLY96
3.083
ALA97
3.349
ARG98
3.118
Residue
Distance (Å)
LEU108
4.768
ASN112
3.990
ILE115
3.368
PHE118
4.956
ILE119
4.064
VAL135
3.149
SER136
3.517
ASN137
2.870
VAL139
3.977
SER160
3.839
GLY161
4.219
LEU164
3.558
ASP165
4.899
HIS192
3.230
TYR246
4.703
THR247
3.511
ILE251
3.500
PDB ID: 4OKN      Crystal structure of human muscle L-lactate dehydrogenase, ternary complex with NADH and oxalate
Method X-ray diffraction Resolution 2.10 Å Mutation No [12]
PDB Sequence
ATLKDQLIYN
11
LLKEEQTPQN
21
KITVVGVGAV
31
GMACAISILM
41
KDLADELALV
51

DVIEDKLKGE
61
MMDLQHGSLF
71
LRTPKIVSGK
81
DYNVTANSKL
91
VIITAGARQQ
101

EGESRLNLVQ
111
RNVNIFKFII
121
PNVVKYSPNC
131
KLLIVSNPVD
141
ILTYVAWKIS
151

GFPKNRVIGS
161
GCNLDSARFR
171
YLMGERLGVH
181
PLSCHGWVLG
191
EHGDSSVPVW
201

SGMNVAGVSL
211
KTLHPDLGTD
221
KDKEQWKEVH
231
KQVVESAYEV
241
IKLKGYTSWA
251

IGLSVADLAE
261
SIMKNLRRVH
271
PVSTMIKGLY
281
GIKDDVFLSV
291
PCILGQNGIS
301

DLVKVTLTSE
311
EEARLKKSAD
321
TLWGIQKELQ
331
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:51 or .A:52 or .A:53 or .A:54 or .A:57 or .A:83 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:109 or .A:113 or .A:116 or .A:119 or .A:120 or .A:136 or .A:137 or .A:138 or .A:140 or .A:161 or .A:165 or .A:193 or .A:247 or .A:248 or .A:252; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL26
3.996
GLY27
4.070
VAL28
4.014
GLY29
3.281
ALA30
3.035
VAL31
2.886
GLY32
4.143
VAL51
4.591
ASP52
2.639
VAL53
3.656
ILE54
3.253
LYS57
4.016
TYR83
4.239
THR95
3.122
ALA96
3.379
GLY97
3.195
ALA98
2.529
Residue
Distance (Å)
ARG99
2.873
GLN100
2.683
LEU109
3.842
ASN113
3.866
ILE116
3.968
PHE119
3.672
ILE120
3.504
VAL136
2.893
SER137
3.946
ASN138
2.995
VAL140
4.006
SER161
3.177
LEU165
3.727
HIS193
2.739
TYR247
4.266
THR248
3.269
ILE252
3.595
PDB ID: 5ZJD      Lactate dehydrogenase with NADH and MLA
Method X-ray diffraction Resolution 2.39 Å Mutation No [13]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:51 or .A:52 or .A:53 or .A:56 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:108 or .A:112 or .A:115 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
4.838
GLY26
4.312
VAL27
3.955
GLY28
3.106
ALA29
2.924
VAL30
2.804
GLY31
4.266
ASP51
2.590
VAL52
3.178
ILE53
3.419
LYS56
2.992
TYR82
4.709
THR94
3.116
ALA95
3.390
GLY96
3.312
ALA97
2.815
Residue
Distance (Å)
ARG98
2.697
GLN99
4.158
LEU108
4.080
ASN112
3.611
ILE115
3.662
ILE119
3.601
VAL135
3.050
SER136
3.807
ASN137
2.914
VAL139
3.953
SER160
3.035
LEU164
3.434
HIS192
3.048
TYR246
4.257
THR247
3.104
ILE251
3.367
PDB ID: 7M2N      Crystal structure of Human Lactate Dehydrogenase A with Inhibitor Compound 15
Method X-ray diffraction Resolution 2.50 Å Mutation No [14]
PDB Sequence
ATLKDQLIYN
10
LLTPQNKITV
24
VGVGAVGMAC
34
AISILMKDLA
44
DELALVDVIE
54

DKLKGEMMDL
64
QHGSLFLRTP
74
KIVSGKDYNV
84
TANSKLVIIT
94
AGARQQEGES
104

RLNLVQRNVN
114
IFKFIIPNVV
124
KYSPNCKLLI
134
VSNPVDILTY
144
VAWKISGFPK
154

NRVIGSGCNL
164
DSARFRYLMG
174
ERLGVHPLSC
184
HGWVLGEHGD
194
SSVPVWSGMN
204

VAGVSLKTLH
214
PDLGTDKDKE
224
QWKEVHKQVV
234
ESAYEVIKLK
244
GYTSWAIGLS
254

VADLAESIMK
264
NLRRVHPVST
274
MIKGLYGIKD
284
DVFLSVPCIL
294
GQNGISDLVK
304

VTLTSEEEAR
314
LKKSADTLWG
324
IQKELQF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:50 or .A:51 or .A:52 or .A:53 or .A:82 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:115 or .A:118 or .A:119 or .A:135 or .A:136 or .A:137 or .A:139 or .A:160 or .A:161 or .A:164 or .A:192 or .A:246 or .A:247 or .A:251; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.837
GLY26
3.896
VAL27
4.051
GLY28
3.418
ALA29
3.220
VAL30
3.017
GLY31
4.380
VAL50
4.572
ASP51
2.602
VAL52
3.427
ILE53
3.376
TYR82
4.112
THR94
3.178
ALA95
3.310
GLY96
3.208
ALA97
4.959
Residue
Distance (Å)
ARG98
2.489
ILE115
3.557
PHE118
4.381
ILE119
3.683
VAL135
3.063
SER136
3.456
ASN137
2.887
VAL139
3.897
SER160
2.958
GLY161
4.406
LEU164
3.807
HIS192
3.141
TYR246
4.293
THR247
3.462
ILE251
3.496
PDB ID: 4L4S      Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme
Method X-ray diffraction Resolution 2.90 Å Mutation No [15]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARQQ
100

EGESRLNLVQ
110
RNVNIFKFII
120
PNVVKYSPNC
130
KLLIVSNPVD
140
ILTYVAWKIS
150

GFPKNRVIGS
160
GCNLDSARFR
170
YLMGERLGVH
180
PLSCHGWVLG
190
EHGDSSVPVW
200

SGMNVAGVSL
210
KTLHPDLGTD
220
KDKEQWKEVH
230
KQVVESAYEV
240
IKLKGYTSWA
250

IGLSVADLAE
260
SIMKNLRRVH
270
PVSTMIKGLY
280
GIKDDVFLSV
290
PCILGQNGIS
300

DLVKVTLTSE
310
EEARLKKSAD
320
TLWGIQKELQ
330
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAI or .NAI2 or .NAI3 or :3NAI;style chemicals stick;color identity;select .H:25 or .H:26 or .H:27 or .H:28 or .H:29 or .H:30 or .H:31 or .H:50 or .H:51 or .H:52 or .H:53 or .H:82 or .H:94 or .H:95 or .H:96 or .H:98 or .H:112 or .H:115 or .H:118 or .H:119 or .H:135 or .H:136 or .H:137 or .H:139 or .H:160 or .H:161 or .H:164 or .H:192 or .H:246 or .H:247 or .H:251; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
4.224
GLY26
3.978
VAL27
3.977
GLY28
3.588
ALA29
3.308
VAL30
2.885
GLY31
4.112
VAL50
4.175
ASP51
2.569
VAL52
3.488
ILE53
3.342
TYR82
3.898
THR94
3.171
ALA95
3.305
GLY96
3.462
ARG98
3.041
Residue
Distance (Å)
ASN112
4.917
ILE115
3.495
PHE118
4.293
ILE119
3.901
VAL135
3.303
SER136
3.692
ASN137
3.245
VAL139
4.635
SER160
3.306
GLY161
4.715
LEU164
3.230
HIS192
3.473
TYR246
4.575
THR247
4.033
ILE251
3.412
References  Top
REF 1 Discovery and Optimization of Potent, Cell-Active Pyrazole-Based Inhibitors of Lactate Dehydrogenase (LDH). J Med Chem. 2017 Nov 22;60(22):9184-9204.
REF 2 Structure-based Optimization of Potent, Cell-Active
REF 3 Pyrazole-Based Lactate Dehydrogenase Inhibitors with Optimized Cell Activity and Pharmacokinetic Properties. J Med Chem. 2020 Oct 8;63(19):10984-11011.
REF 4 Structure-based Optimization of Potent, Cell-Active
REF 5 Structural Evidence for Isoform-Selective Allosteric Inhibition of Lactate Dehydrogenase A. ACS Omega. 2020 May 27;5(22):13034-13041.
REF 6 Identification of substituted 2-thio-6-oxo-1,6-dihydropyrimidines as inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett. 2013 Jun 1;23(11):3186-94.
REF 7 Identification of 3,6-disubstituted dihydropyrones as inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett. 2014 Dec 15;24(24):5683-5687.
REF 8 Identification of substituted 3-hydroxy-2-mercaptocyclohex-2-enones as potent inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett. 2014 Aug 15;24(16):3764-71.
REF 9 Identification of 2-amino-5-aryl-pyrazines as inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett. 2013 Oct 15;23(20):5533-9.
REF 10 Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enones as potent inhibitors of human lactate dehydrogenase. Bioorg Med Chem Lett. 2015 Jan 1;25(1):75-82.
REF 11 Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins. 2001 May 1;43(2):175-85.
REF 12 Structures of lactate dehydrogenase A (LDHA) in apo, ternary and inhibitor-bound forms. Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):185-95.
REF 13 Machilin A Inhibits Tumor Growth and Macrophage M2 Polarization Through the Reduction of Lactic Acid. Cancers (Basel). 2019 Jul 9;11(7):963.
REF 14 Dual Glycolate Oxidase/Lactate Dehydrogenase A Inhibitors for Primary Hyperoxaluria. doi:10.1021/acsmedchemlett.1c00196.
REF 15 Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1484-90.

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