Structure of PDB 4mpg Chain A

Receptor sequence
>4mpgA (length=243) Species: 9606 (Homo sapiens) [Search protein sequence]
GLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSL
GKLPTLKDGDFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGW
HADCIRGTFGIPLWVQVLGPLIGVQVPKEKVERNRTAMDQALQWLEDKFL
GDRPFLAGQQVTLADLMALEELMQPVALGYELFEGRPRLAAWRGRVEAFL
GAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRIARIP
3D structure
PDB4mpg Crystal Structure of Human Glutathione S-Transferase Theta-2 (Target EFI-507257)
ChainA
Resolution1.951 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S11 S14 I48 N49
Catalytic site (residue number reindexed from 1) S10 S13 I47 N48
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 GSH A S11 P13 H40 K41 K53 L54 E66 S67 R107 S10 P12 H39 K40 K52 L53 E65 S66 R106
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0005515 protein binding
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
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:4mpg, PDBe:4mpg, PDBj:4mpg
PDBsum4mpg
PubMed
UniProtP0CG30|GSTT2_HUMAN Glutathione S-transferase theta-2B (Gene Name=GSTT2B)

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