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 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: 4ZVV      Lactate dehydrogenase A in complex with a trisubstituted piperidine-2,4-dione inhibitor GNE-140
Method X-ray diffraction Resolution 2.20 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
4.152
GLY26
4.011
VAL27
4.121
GLY28
3.557
ALA29
3.420
VAL30
3.188
GLY31
4.375
VAL50
4.559
ASP51
2.612
VAL52
3.490
ILE53
3.328
TYR82
4.325
THR94
3.058
ALA95
3.272
GLY96
3.402
ARG98
3.069
Residue
Distance (Å)
ASN112
4.992
ILE115
3.156
PHE118
4.721
ILE119
3.876
VAL135
3.079
SER136
3.925
ASN137
2.641
VAL139
4.014
SER160
4.368
GLY161
4.704
LEU164
3.595
HIS192
3.205
TYR246
4.470
THR247
3.816
ILE251
3.516
PDB ID: 6BB0      Lactate Dehydrogenase in complex with inhibitor (R)-3-((2-chlorophenyl)thio)-6-(3-((4-fluorophenyl)amino)phenyl)-4-hydroxy-6-(thiophen-3-yl)-5,6-dihydro-2H-pyran-2-one
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: 6BAX      Lactate Dehydrogenase in complex with inhibitor 6-(3-aminophenyl)-3-((2-chlorophenyl)thio)-4-hydroxy-6-(thiophen-3-yl)-5,6-dihydro-2H-pyran-2-one
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
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
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: 6BAD      Lactate Dehydrogenase in complex with inhibitor (R)-3-((2-chlorophenyl)thio)-6-(3-((4-fluorophenyl)amino)phenyl)-4-hydroxy-6-(thiophen-3-yl)-5,6-dihydro-2H-pyran-2-one
Method X-ray diffraction Resolution 2.10 Å Mutation No [4]
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 .NAD or .NAD2 or .NAD3 or :3NAD;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: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
3.829
GLY26
3.778
VAL27
3.797
GLY28
3.262
ALA29
3.144
VAL30
2.871
GLY31
4.368
VAL50
4.513
ASP51
2.716
VAL52
3.514
ILE53
3.263
LYS56
3.746
TYR82
4.283
THR94
3.515
ALA95
3.565
GLY96
3.053
ALA97
3.390
Residue
Distance (Å)
ARG98
2.954
GLN99
4.915
ASN112
4.380
ILE115
3.505
PHE118
4.962
ILE119
3.705
VAL135
3.111
SER136
3.485
ASN137
2.835
VAL139
3.908
SER160
3.850
GLY161
4.376
LEU164
3.775
HIS192
3.100
TYR246
4.315
THR247
3.362
ILE251
3.526
PDB ID: 6BB1      Lactate Dehydrogenase in complex with inhibitor (R)-5-((2-chlorophenyl)thio)-6'-(4-fluorophenoxy)-4-hydroxy-2-(thiophen-3-yl)-2,3-dihydro-[2,2'-bipyridin]-6(1H)-one
Method X-ray diffraction Resolution 2.30 Å Mutation No [5]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGARNL
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
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: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: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
3.885
GLY26
3.934
VAL27
4.052
GLY28
3.259
ALA29
3.173
VAL30
2.940
GLY31
4.265
VAL50
4.482
ASP51
2.680
VAL52
3.556
ILE53
3.313
LYS56
2.939
TYR82
4.186
THR94
3.093
ALA95
3.559
GLY96
2.994
ALA97
3.912
Residue
Distance (Å)
ARG98
2.909
LEU108
4.823
ASN112
4.202
ILE115
3.670
PHE118
4.528
ILE119
3.492
VAL135
3.106
SER136
3.597
ASN137
3.016
VAL139
4.115
SER160
3.026
GLY161
4.716
LEU164
3.614
HIS192
3.172
TYR246
4.367
THR247
3.160
ILE251
3.585
PDB ID: 6BAG      Lactate Dehydrogenase in complex with inhibitor (R)-5-((2-chlorophenyl)thio)-6'-((4-fluorophenyl)amino)-4-hydroxy-2-(thiophen-3-yl)-2,3-dihydro-[2,2'-bipyridin]-6(1H)-one
Method X-ray diffraction Resolution 2.40 Å Mutation No [6]
PDB Sequence
ATLKDQLIYN
10
LLKEEQTPQN
20
KITVVGVGAV
30
GMACAISILM
40
KDLADELALV
50

DVIEDKLKGE
60
MMDLQHGSLF
70
LRTPKIVSGK
80
DYNVTANSKL
90
VIITAGAGES
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 .NAD or .NAD2 or .NAD3 or :3NAD;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 #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL25
3.883
GLY26
3.902
VAL27
4.016
GLY28
3.396
ALA29
3.311
VAL30
3.069
GLY31
4.423
VAL50
4.581
ASP51
2.731
VAL52
3.502
ILE53
3.251
TYR82
4.217
THR94
3.227
ALA95
3.294
GLY96
3.382
Residue
Distance (Å)
ILE115
3.517
PHE118
4.478
ILE119
3.569
VAL135
3.052
SER136
3.617
ASN137
2.853
VAL139
3.935
SER160
3.926
GLY161
4.433
LEU164
3.568
HIS192
3.204
TYR246
4.360
THR247
3.247
ILE251
3.405
PDB ID: 6BB3      Lactate Dehydrogenase in complex with inhibitor 3-((2-chlorophenyl)thio)-6-(6-((4-fluorophenyl)amino)pyridin-2-yl)-4-hydroxy-6-(thiophen-3-yl)-5,6-dihydro-2H-pyran-2-one
Method X-ray diffraction Resolution 2.40 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 .NAD or .NAD2 or .NAD3 or :3NAD;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: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
3.913
GLY26
3.816
VAL27
3.918
GLY28
3.309
ALA29
3.205
VAL30
3.047
GLY31
4.423
VAL50
4.562
ASP51
2.680
VAL52
3.590
ILE53
3.277
LYS56
4.010
TYR82
4.362
THR94
3.235
ALA95
3.444
GLY96
3.734
Residue
Distance (Å)
ALA97
4.804
ARG98
2.790
ILE115
3.715
PHE118
4.618
ILE119
3.552
VAL135
2.973
SER136
3.809
ASN137
2.840
VAL139
4.144
SER160
4.009
GLY161
4.525
LEU164
3.839
HIS192
3.015
TYR246
4.276
THR247
3.391
ILE251
3.527
PDB ID: 6BB2      Lactate Dehydrogenase in complex with inhibitor (S)-5-((2-chlorophenyl)thio)-6'-(4-fluorophenoxy)-4-hydroxy-2-(thiophen-3-yl)-2,3-dihydro-[2,2'-bipyridin]-6(1H)-one
Method X-ray diffraction Resolution 2.47 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 .NAD or .NAD2 or .NAD3 or :3NAD;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: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
3.947
GLY26
3.986
VAL27
4.054
GLY28
3.328
ALA29
3.283
VAL30
2.955
GLY31
4.260
VAL50
4.514
ASP51
2.718
VAL52
3.597
ILE53
3.340
LYS56
3.107
TYR82
4.135
THR94
3.073
ALA95
3.426
GLY96
3.308
ALA97
2.835
ARG98
3.095
Residue
Distance (Å)
GLN99
4.332
LEU108
4.133
ASN112
3.997
ILE115
3.906
PHE118
4.457
ILE119
3.550
VAL135
2.916
SER136
3.597
ASN137
3.011
VAL139
3.937
SER160
3.123
GLY161
4.813
LEU164
3.490
HIS192
3.069
TYR246
4.345
THR247
3.204
ILE251
3.261
PDB ID: 6BAZ      Lactate Dehydrogenase in complex with inhibitor (S)-5-((2-chlorophenyl)thio)-6'-((4-fluorophenyl)amino)-4-hydroxy-2-(thiophen-3-yl)-2,3-dihydro-[2,2'-bipyridin]-6(1H)-one
Method X-ray diffraction Resolution 2.70 Å Mutation No [9]
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 .NAD or .NAD2 or .NAD3 or :3NAD;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
3.877
GLY26
3.955
VAL27
4.066
GLY28
3.278
ALA29
3.085
VAL30
2.992
GLY31
4.321
VAL50
4.256
ASP51
2.706
VAL52
3.498
ILE53
3.344
TYR82
4.118
THR94
3.206
ALA95
3.423
GLY96
3.113
ALA97
3.454
Residue
Distance (Å)
ARG98
2.964
ILE115
3.431
PHE118
4.877
ILE119
3.993
VAL135
3.104
SER136
3.896
ASN137
2.863
VAL139
4.073
SER160
3.018
GLY161
4.603
LEU164
3.445
HIS192
3.176
TYR246
4.407
THR247
3.152
ILE251
3.384
PDB ID: 5IXY      Lactate Dehydrogenase in complex with hydroxylactam inhibitor compound 31: (2~{S})-5-(2-chlorophenyl)sulfanyl-2-(4-morpholin-4-ylphenyl)-4-oxidanyl-2-thiophen-3-yl-1,3-dihydropyridin-6-one
Method X-ray diffraction Resolution 3.00 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 .NAD or .NAD2 or .NAD3 or :3NAD;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: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
3.741
GLY26
3.954
VAL27
3.921
GLY28
3.400
ALA29
3.220
VAL30
3.126
GLY31
4.082
VAL50
4.386
ASP51
2.710
VAL52
3.504
ILE53
3.264
LYS56
2.768
TYR82
3.778
THR94
3.208
ALA95
3.374
GLY96
3.474
Residue
Distance (Å)
ALA97
4.965
ARG98
3.229
ILE115
3.607
PHE118
4.037
ILE119
3.474
VAL135
2.807
SER136
3.535
ASN137
2.817
VAL139
4.152
SER160
4.007
GLY161
4.578
LEU164
3.623
HIS192
3.081
TYR246
4.454
THR247
4.479
ILE251
3.391
References  Top
REF 1 Metabolic plasticity underpins innate and acquired resistance to LDHA inhibition. Nat Chem Biol. 2016 Oct;12(10):779-86.
REF 2 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 3 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 4 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 5 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 6 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 7 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 8 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 9 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 10 Cell Active Hydroxylactam Inhibitors of Human Lactate Dehydrogenase with Oral Bioavailability in Mice. ACS Med Chem Lett. 2016 Aug 26;7(10):896-901.

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