Structure of PDB 2wp5 Chain A Binding Site BS02

Receptor Information
>2wp5 Chain A (length=488) Species: 185431 (Trypanosoma brucei brucei TREU927) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMSKAFDLVVIGAGSGGLEAGWNAATLYGKRVAVVDVQTSHGPPFYAALG
GTCVNVGCVPKKLMVTGAQYMDHLRESAGFGWEFDGSSVKANWKKLIAAK
NEAVLDINKSYEGMFNDTEGLDFFLGWGSLESKNVVVVRETADPKSAVKE
RLQADHILLATGSWPQMPAIPGIEHCISSNEAFYLPEPPRRVLTVGGGFI
SVEFAGIFNAYKPPGGKVTLCYRNNLILRGFDETIREEVTKQLTANGIEI
MTNENPAKVSLNTDGSKHVTFESGKTLDVDVVMMAIGRIPRTNDLQLGNV
GVKLTPKGGVQVDEFSRTNVPNIYAIGDITDRLMLTPVAINEGAALVDTV
FGNKPRKTDHTRVASAVFSIPPIGTCGLIEEVAAKEFEKVAVYMSSFTPL
MHNISGSKYKKFVAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRLNA
KISDFYNTIGVHPTSAEELCSMRTPSYYYVKGEKMEKL
Ligand information
Ligand IDWP5
InChIInChI=1S/C18H17BrN2O2/c1-12-20-16-9-8-14(19)10-15(16)18(13-6-4-3-5-7-13)21(12)11-17(22)23-2/h3-10,18H,11H2,1-2H3/t18-/m0/s1
InChIKeyZWSKQYINLNUCMK-SFHVURJKSA-N
SMILES
SoftwareSMILES
CACTVS 3.352COC(=O)CN1[CH](c2ccccc2)c3cc(Br)ccc3N=C1C
ACDLabs 10.04Brc2ccc1N=C(N(C(c1c2)c3ccccc3)CC(=O)OC)C
OpenEye OEToolkits 1.6.1CC1=Nc2ccc(cc2C(N1CC(=O)OC)c3ccccc3)Br
CACTVS 3.352COC(=O)CN1[C@@H](c2ccccc2)c3cc(Br)ccc3N=C1C
OpenEye OEToolkits 1.6.1CC1=Nc2ccc(cc2[C@@H](N1CC(=O)OC)c3ccccc3)Br
FormulaC18 H17 Br N2 O2
NameMETHYL [(4S)-6-BROMO-2-METHYL-4-PHENYLQUINAZOLIN-3(4H)-YL]ACETATE
ChEMBL
DrugBank
ZINCZINC000000655345
PDB chain2wp5 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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PDB2wp5 Dihydroquinazolines as a Novel Class of Trypanosoma Brucei Trypanothione Reductase Inhibitors: Discovery, Synthesis, and Characterization of Their Binding Mode by Protein Crystallography.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		S14 L17 E18 W21 Y110 M113
Binding residue
(residue number reindexed from 1)		S15 L18 E19 W22 Y111 M114
Annotation score1
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) S15 L49 C53 C58 K61 G86 S87 F199 E203 I340 G460 H462 E467 E486 K487
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:2wp5, PDBe:2wp5, PDBj:2wp5
PDBsum2wp5
PubMed21851087
UniProtQ389T8

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