Structure of PDB 2wpe Chain A Binding Site BS02

Receptor Information
>2wpe Chain A (length=490) Species: 185431 (Trypanosoma brucei brucei TREU927) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SHMSKAFDLVVIGAGSGGLEAGWNAATLYGKRVAVVDVQTSHGPPFYAAL
GGTCVNVGCVPKKLMVTGAQYMDHLRESAGFGWEFDGSSVKANWKKLIAA
KNEAVLDINKSYEGMFNDTEGLDFFLGWGSLESKNVVVVRETADPKSAVK
ERLQADHILLATGSWPQMPAIPGIEHCISSNEAFYLPEPPRRVLTVGGGF
ISVEFAGIFNAYKPPGGKVTLCYRNNLILRGFDETIREEVTKQLTANGIE
IMTNENPAKVSLNTDGSKHVTFESGKTLDVDVVMMAIGRIPRTNDLQLGN
VGVKLTPKGGVQVDEFSRTNVPNIYAIGDITDRLMLTPVAINEGAALVDT
VFGNKPRKTDHTRVASAVFSIPPIGTCGLIEEVAAKEFEKVAVYMSSFTP
LMHNISGSKYKKFVAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRLN
AKISDFYNTIGVHPTSAEELCSMRTPSYYYVKGEKMEKLP
Ligand information
Ligand IDWPE
InChIInChI=1S/C22H20ClN3O2/c1-15-25-19-10-9-17(23)14-18(19)21(16-6-3-2-4-7-16)26(15)12-11-24-22(27)20-8-5-13-28-20/h2-10,13-14,21H,11-12H2,1H3,(H,24,27)/t21-/m0/s1
InChIKeyIPLMZBHGWQTVKV-NRFANRHFSA-N
SMILES
SoftwareSMILES
CACTVS 3.352CC1=Nc2ccc(Cl)cc2[CH](N1CCNC(=O)c3occc3)c4ccccc4
OpenEye OEToolkits 1.6.1CC1=Nc2ccc(cc2C(N1CCNC(=O)c3ccco3)c4ccccc4)Cl
CACTVS 3.352CC1=Nc2ccc(Cl)cc2[C@@H](N1CCNC(=O)c3occc3)c4ccccc4
OpenEye OEToolkits 1.6.1CC1=Nc2ccc(cc2[C@@H](N1CCNC(=O)c3ccco3)c4ccccc4)Cl
ACDLabs 10.04O=C(NCCN3C(=Nc1ccc(Cl)cc1C3c2ccccc2)C)c4occc4
FormulaC22 H20 Cl N3 O2
NameN-{2-[(4S)-6-CHLORO-2-METHYL-4-PHENYLQUINAZOLIN-3(4H)-YL]ETHYL}FURAN-2-CARBOXAMIDE
ChEMBL
DrugBank
ZINCZINC000058650442
PDB chain2wpe Chain A Residue 1000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2wpe Dihydroquinazolines as a Novel Class of Trypanosoma Brucei Trypanothione Reductase Inhibitors: Discovery, Synthesis, and Characterization of Their Binding Mode by Protein Crystallography.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		L17 E18 W21 Y110 M113 F114
Binding residue
(residue number reindexed from 1)		L19 E20 W23 Y112 M115 F116
Annotation score1
Binding affinityMOAD: ic50=0.86uM
Enzymatic activity
Catalytic site (original residue number in PDB) S14 L48 C52 C57 K60 G85 S86 F198 E202 I339 G459 H461 E466 E485 K486
Catalytic site (residue number reindexed from 1) S16 L50 C54 C59 K62 G87 S88 F200 E204 I341 G461 H463 E468 E487 K488
Enzyme Commision number 1.8.1.12: trypanothione-disulfide reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
GO:0015036 disulfide oxidoreductase activity
GO:0015042 trypanothione-disulfide reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0020015 glycosome
GO:0097014 ciliary plasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2wpe, PDBe:2wpe, PDBj:2wpe
PDBsum2wpe
PubMed21851087
UniProtQ389T8

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