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 Lactic Acid Ligand Info
Canonical SMILES CC(C(=O)O)O
InChI 1S/C3H6O3/c1-2(4)3(5)6/h2,4H,1H3,(H,5,6)
InChIKey JVTAAEKCZFNVCJ-UHFFFAOYSA-N
PubChem Compound ID 612
Drug Binding Sites of Target  Top
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 [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)
GLN99
3.052
ARG105
3.034
ASN137
2.705
LEU164
3.730
ARG168
2.872
Residue
Distance (Å)
HIS192
2.958
ALA237
3.512
ILE241
4.325
THR247
2.803
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 [2]
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
Residue
Distance (Å)
ASN137
2.782
LEU164
3.974
ARG168
3.165
HIS192
3.284
Residue
Distance (Å)
ALA237
3.816
ILE241
3.855
THR247
3.154
References  Top
REF 1 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase
REF 2 Structure-guided optimization and in vivo activities of hydroxylactone and hydroxylactam Inhibitors of Human Lactate Dehydrogenase

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