Structure of PDB 4nev Chain B Binding Site BS03

Receptor Information
>4nev Chain B (length=485) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KAFDLVVIGAGSGGLEAGWNAATLYGKRVAVVDVQTSHGPPFYAALGGTC
VNVGCVPKKLMVTGAQYMDHLRESAGFGWEFDGSSVKANWKKLIAAKNEA
VLDINKSYEGMFNDTEGLDFFLGWGSLESKNVVVVRETADPKSAVKERLQ
ADHILLATGSWPQMPAIPGIEHCISSNEAFYLPEPPRRVLTVGGGFISVE
FAGIFNAYKPPGGKVTLCYRNNLILRGFDETIREEVTKQLTANGIEIMTN
ENPAKVSLNTDGSKHVTFESGKTLDVDVVMMAIGRIPRTNDLQLGNVGVK
LTPKGGVQVDEFSRTNVPNIYAIGDITDRLMLTPVAINEGAALVDTVFGN
KPRKTDHTRVASAVFSIPPIGTCGLIEEVAAKEFEKVAVYMSSFTPLMHN
ISGSKYKKFVAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRLNAKIS
DFYNTIGVHPTSAEELCSMRTPSYYYVKGEKMEKL
Ligand information
Ligand ID2JR
InChIInChI=1S/C21H25N3S/c1-2-9-21(10-3-1,24-12-4-5-13-24)19-15-23-20(25-19)17-6-7-18-16(14-17)8-11-22-18/h6-8,11,14-15,22H,1-5,9-10,12-13H2
InChIKeyMXBHIYKTGVOQMD-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01n1cc(sc1c3cc2ccnc2cc3)C5(N4CCCC4)CCCCC5
CACTVS 3.385C1CCC(CC1)(N2CCCC2)c3sc(nc3)c4ccc5[nH]ccc5c4
OpenEye OEToolkits 1.7.6c1cc2c(cc[nH]2)cc1c3ncc(s3)C4(CCCCC4)N5CCCC5
FormulaC21 H25 N3 S
Name5-{5-[1-(pyrrolidin-1-yl)cyclohexyl]-1,3-thiazol-2-yl}-1H-indole
ChEMBL
DrugBank
ZINCZINC000098208183
PDB chain4nev Chain B Residue 509 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4nev Binding to large enzyme pockets: small-molecule inhibitors of trypanothione reductase.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		P42 Y183
Binding residue
(residue number reindexed from 1)		P40 Y181
Annotation score1
Binding affinityMOAD: Ki=12uM
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) S12 L46 C50 C55 K58 G83 S84 F196 E200 I337 G457 H459 E464 E483 K484
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:4nev, PDBe:4nev, PDBj:4nev
PDBsum4nev
PubMed24788386
UniProtQ389T8

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