Structure of PDB 1gxf Chain A Binding Site BS02

Receptor Information
>1gxf Chain A (length=484) Species: 5693 (Trypanosoma cruzi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIFDLVVIGAGSGGLEAAWNAATLYKKRVAVIDVQMVHGPPFFSALGGTC
VNVGCVPKKLMVTGAQYMEHLRESAGFGWEFDRTTLRAEWKNLIAVKDEA
VLNINKSYDEMFRDTEGLEFFLGWGSLESKNVVNVRESADPASAVKERLE
TEHILLASGSWPHMPNIPGIEHCISSNEAFYLPEPPRRVLTVGGGFISVE
FAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELTKQLTANGIQILTK
ENPAKVELNADGSKSVTFESGKKMDFDLVMMAIGRSPRTKDLQLQNAGVM
IKNGGVQVDEYSRTNVSNIYAIGDVTNRVMLTPVAINEAAALVDTVFGTT
PRKTDHTRVASAVFSIPPIGTCGLIEEVASKRYEVVAVYLSSFTPLMHKV
SGSKYKTFVAKIITNHSDGTVLGVHLLGDNAPEIIQGIGICLKLNAKISD
FYNTIGVHPTSAEELCSMRTPSYYYVKGEKMEKP
Ligand information
Ligand IDQUM
InChIInChI=1S/C23H28Cl3N3O/c1-16(4-3-11-29(12-9-24)13-10-25)27-23-19-7-5-17(26)14-22(19)28-21-8-6-18(30-2)15-20(21)23/h5-8,14-16H,3-4,9-13H2,1-2H3,(H,27,28)/t16-/m0/s1
InChIKeyUKOBAUFLOGFCMV-INIZCTEOSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COc1ccc2Nc3cc(Cl)ccc3C(=N[C@@H](C)CCCN(CCCl)CCCl)c2c1
OpenEye OEToolkits 1.5.0CC(CCCN(CCCl)CCCl)N=C1c2ccc(cc2Nc3c1cc(cc3)OC)Cl
OpenEye OEToolkits 1.5.0C[C@@H](CCCN(CCCl)CCCl)/N=C\1/c2ccc(cc2Nc3c1cc(cc3)OC)Cl
ACDLabs 10.04ClCCN(CCCl)CCCC(/N=C2\c1c(ccc(OC)c1)Nc3c2ccc(Cl)c3)C
CACTVS 3.341COc1ccc2Nc3cc(Cl)ccc3C(=N[CH](C)CCCN(CCCl)CCCl)c2c1
FormulaC23 H28 Cl3 N3 O
NameQUINACRINE MUSTARD;
N-{(1S)-4-[BIS(2-CHLOROETHYL)AMINO]-1-METHYLBUTYL}-N-(6-CHLORO-2-METHOXY-9-ACRIDINYL)AMINE
ChEMBL
DrugBank
ZINCZINC000004404007
PDB chain1gxf Chain A Residue 1501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1gxf Two Interacting Binding Sites for Quinacrine Derivatives in the Active Site of Trypanothione Reductase: A Template for Drug Design
Resolution2.7 Å
Binding residue
(original residue number in PDB)		L18 E19 W22 S110 Y111 E113 M114 D117
Binding residue
(residue number reindexed from 1)		L15 E16 W19 S107 Y108 E110 M111 D114
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S15 L49 C53 C58 K61 R86 T87 F199 E203 I339 G459 H461 E466 E485 K486
Catalytic site (residue number reindexed from 1) S12 L46 C50 C55 K58 R83 T84 F196 E200 I336 G456 H458 E463 E482 K483
Enzyme Commision number 1.8.1.12: trypanothione-disulfide reductase.
Gene Ontology
Molecular Function
GO:0004362 glutathione-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:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0034599 cellular response to oxidative stress
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1gxf, PDBe:1gxf, PDBj:1gxf
PDBsum1gxf
PubMed15102853
UniProtP28593|TYTR_TRYCR Trypanothione reductase (Gene Name=TPR)

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