Structure of PDB 4ajl Chain B Binding Site BS01

Receptor Information
>4ajl Chain B (length=328) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALKDQLIVNLLKQVPQNKITVVGVGAVGMACAISILMKDLADELALVDVI
EDKLKGEMMDLQHGSLFLKTPKIVSSKDYSVTANSKLVIITAGARQQEGE
SRLNLVQRNVNIFKFIIPNVVKYSPQCKLLIVSNPVDILTYVAWKISGFP
KNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGV
NVAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVIKLKGYTSWAIGL
SVADLAESIMKNLRRVHPISTMIKGLYGIKEDVFLSVPCILGQNGISDVV
KVTLTPDEEARLKKSADTLWGIQKELQF
Ligand information
Ligand ID88W
InChIInChI=1S/C14H18N4O2S/c1-3-15-14(20)16-7-6-13(19)18-10-4-5-11-12(8-10)21-9(2)17-11/h4-5,8H,3,6-7H2,1-2H3,(H,18,19)(H2,15,16,20)
InChIKeyFBTWWPKAGBUCIB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CCNC(=O)NCCC(=O)Nc1ccc2nc(C)sc2c1
OpenEye OEToolkits 1.9.2CCNC(=O)NCCC(=O)Nc1ccc2c(c1)sc(n2)C
ACDLabs 12.01O=C(NCC)NCCC(=O)Nc1ccc2nc(sc2c1)C
FormulaC14 H18 N4 O2 S
NameN~3~-(ethylcarbamoyl)-N-(2-methyl-1,3-benzothiazol-6-yl)-beta-alaninamide;
3-(ETHYLCARBAMOYLAMINO)-N-(2-METHYL-1,3-BENZOTHIAZOL-6-
ChEMBLCHEMBL2059006
DrugBank
ZINCZINC000084726902
PDB chain4ajl Chain B Residue 1333 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4ajl The Design and Synthesis of Novel Lactate Dehydrogenase a Inhibitors by Fragment-Based Lead Generation
Resolution1.77 Å
Binding residue
(original residue number in PDB)		D51 V52 T94 A95 G96 R98 I115 I119
Binding residue
(residue number reindexed from 1)		D48 V49 T91 A92 G93 R95 I112 I116
Annotation score1
Binding affinityMOAD: Kd=160uM
BindingDB: Kd=1.60e+5nM,IC50=>5.00e+5nM
Enzymatic activity
Catalytic site (original residue number in PDB) R105 D165 R168 H192
Catalytic site (residue number reindexed from 1) R102 D162 R165 H189
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004457 lactate dehydrogenase activity
GO:0004459 L-lactate dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0019900 kinase binding
GO:0042802 identical protein binding
GO:0051287 NAD binding
Biological Process
GO:0001666 response to hypoxia
GO:0001889 liver development
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0007519 skeletal muscle tissue development
GO:0007584 response to nutrient
GO:0009410 response to xenobiotic stimulus
GO:0009749 response to glucose
GO:0014070 response to organic cyclic compound
GO:0019661 glucose catabolic process to lactate via pyruvate
GO:0019674 NAD metabolic process
GO:0019752 carboxylic acid metabolic process
GO:0042542 response to hydrogen peroxide
GO:0042867 pyruvate catabolic process
GO:0043065 positive regulation of apoptotic process
GO:0043627 response to estrogen
GO:0051591 response to cAMP
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0035686 sperm fibrous sheath
GO:1990204 oxidoreductase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4ajl, PDBe:4ajl, PDBj:4ajl
PDBsum4ajl
PubMed22417091
UniProtP04642|LDHA_RAT L-lactate dehydrogenase A chain (Gene Name=Ldha)

[Back to BioLiP]