Structure of PDB 4ajj Chain C Binding Site BS01

Receptor Information
>4ajj Chain C (length=330) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALKDQLIVNLLKEEQVPQNKITVVGVGAVGMACAISILMKDLADELALVD
VIEDKLKGEMMDLQHGSLFLKTPKIVSSKDYSVTANSKLVIITAGARQQE
GESRLNLVQRNVNIFKFIIPNVVKYSPQCKLLIVSNPVDILTYVAWKISG
FPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWS
GVNVAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVIKLKGYTSWAI
GLSVADLAESIMKNLRRVHPISTMIKGLYGIKEDVFLSVPCILGQNGISD
VVKVTLTPDEEARLKKSADTLWGIQKELQF
Ligand information
Ligand ID88S
InChIInChI=1S/C12H14N4O2S/c1-7-15-9-3-2-8(6-10(9)19-7)16-11(17)4-5-14-12(13)18/h2-3,6H,4-5H2,1H3,(H,16,17)(H3,13,14,18)
InChIKeyOVXHZNUBLPBIEB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.9.2Cc1nc2ccc(cc2s1)NC(=O)CCNC(=O)N
ACDLabs 12.01O=C(N)NCCC(=O)Nc1ccc2nc(sc2c1)C
CACTVS 3.385Cc1sc2cc(NC(=O)CCNC(N)=O)ccc2n1
FormulaC12 H14 N4 O2 S
NameN-(2-METHYL-1,3-BENZOTHIAZOL-6-YL)-3-UREIDO-PROPANAMIDE
ChEMBLCHEMBL2059004
DrugBank
ZINC
PDB chain4ajj Chain C Residue 1334 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4ajj The Design and Synthesis of Novel Lactate Dehydrogenase a Inhibitors by Fragment-Based Lead Generation
Resolution1.75 Å
Binding residue
(original residue number in PDB)		D51 V52 A95 G96 I119
Binding residue
(residue number reindexed from 1)		D50 V51 A94 G95 I118
Annotation score1
Binding affinityMOAD: Kd=770uM
BindingDB: Kd=7.70e+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) R104 D164 R167 H191
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4ajj, PDBe:4ajj, PDBj:4ajj
PDBsum4ajj
PubMed22417091
UniProtP04642|LDHA_RAT L-lactate dehydrogenase A chain (Gene Name=Ldha)

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