Structure of PDB 5hwl Chain A Binding Site BS02

Receptor Information
>5hwl Chain A (length=217) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILE
NQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGD
KITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSS
RFLPRPVFTKMAVWGNK
Ligand information
Ligand IDNNE
InChIInChI=1S/C30H32Cl4N2O6/c1-5-17(3)29(39)19-9-11-21(27(33)25(19)31)41-15-23(37)35-13-7-8-14-36-24(38)16-42-22-12-10-20(26(32)28(22)34)30(40)18(4)6-2/h9-12H,3-8,13-16H2,1-2H3,(H,35,37)(H,36,38)
InChIKeyDJUYDJABFNZJNL-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01C=C(/C(c1ccc(c(c1Cl)Cl)OCC(=O)NCCCCNC(COc2ccc(c(c2Cl)Cl)C(=O)/C(CC)=C)=O)=O)CC
OpenEye OEToolkits 2.0.5CCC(=C)C(=O)c1ccc(c(c1Cl)Cl)OCC(=O)NCCCCNC(=O)COc2ccc(c(c2Cl)Cl)C(=O)C(=C)CC
CACTVS 3.385CCC(=C)C(=O)c1ccc(OCC(=O)NCCCCNC(=O)COc2ccc(c(Cl)c2Cl)C(=O)C(=C)CC)c(Cl)c1Cl
FormulaC30 H32 Cl4 N2 O6
NameN,N'-(butane-1,4-diyl)bis{2-[2,3-dichloro-4-(2-methylidenebutanoyl)phenoxy]acetamide}
ChEMBL
DrugBank
ZINC
PDB chain5hwl Chain B Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5hwl Human glutathione s-transferase Mu2 complexed with BDEA, monoclinic crystal form
Resolution1.6 Å
Binding residue
(original residue number in PDB)		M104 D105 M108
Binding residue
(residue number reindexed from 1)		M104 D105 M108
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y6 L12 R17
Catalytic site (residue number reindexed from 1) Y6 L12 R17
Enzyme Commision number 2.5.1.18: glutathione transferase.
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004602 glutathione peroxidase activity
GO:0005102 signaling receptor binding
GO:0005504 fatty acid binding
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0019899 enzyme binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006749 glutathione metabolic process
GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
GO:0014809 regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
GO:0018916 nitrobenzene metabolic process
GO:0042178 xenobiotic catabolic process
GO:0043651 linoleic acid metabolic process
GO:0051122 hepoxilin biosynthetic process
GO:0055119 relaxation of cardiac muscle
GO:0060315 negative regulation of ryanodine-sensitive calcium-release channel activity
GO:0060316 positive regulation of ryanodine-sensitive calcium-release channel activity
GO:0070458 cellular detoxification of nitrogen compound
GO:0071313 cellular response to caffeine
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016529 sarcoplasmic reticulum
GO:0045171 intercellular bridge
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5hwl, PDBe:5hwl, PDBj:5hwl
PDBsum5hwl
PubMed
UniProtP28161|GSTM2_HUMAN Glutathione S-transferase Mu 2 (Gene Name=GSTM2)

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