Structure of PDB 3rpn Chain B

Receptor sequence
>3rpnB (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.
ChainB
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 B L15 S16 P17 Y18 N53 P56 M91 L92 G182 L183 F198 G199 S200 D201 L14 S15 P16 Y17 N52 P55 M90 L91 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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