Structure of PDB 3rpn Chain E

Receptor sequence
>3rpnE (length=220) Species: 9606 (Homo sapiens) [Search protein sequence]
GPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDS
GNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMR
FLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQ
AQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSD
RMELLAHLLGEKWMGPIPPA
3D structure
PDB3rpn Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism.
ChainE
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.18: glutathione transferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GTX E S16 P17 Y18 N53 M66 L88 G182 L183 F198 G199 S200 D201 S15 P16 Y17 N52 M65 L87 G181 L182 F197 G198 S199 D200
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004602 glutathione peroxidase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0030855 epithelial cell differentiation
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3rpn, PDBe:3rpn, PDBj:3rpn
PDBsum3rpn
PubMed21728995
UniProtQ9Y2Q3|GSTK1_HUMAN Glutathione S-transferase kappa 1 (Gene Name=GSTK1)

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