Structure of PDB 3ljr Chain B

Receptor sequence
>3ljrB (length=244) Species: 9606 (Homo sapiens) [Search protein sequence]
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINS
LGKLPTLKDGDFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLG
WHADCIRGTFGIPLWVQVLGPLIGVQVPEEKVERNRTAMDQALQWLEDKF
LGDRPFLAGQQVTLADLMALEELMQPVALGYELFEGRPRLAAWRGRVEAF
LGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRIARIP
3D structure
PDB3ljr Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.
ChainB
Resolution3.3 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
Catalytic site (residue number reindexed from 1) S11
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 SO4 B Q12 W115 R239 Q12 W115 R239
BS02 GGC B V10 S11 Q12 P13 L35 H40 K41 K53 L54 E66 S67 W115 L119 V10 S11 Q12 P13 L35 H40 K41 K53 L54 E66 S67 W115 L119
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:3ljr, PDBe:3ljr, PDBj:3ljr
PDBsum3ljr
PubMed9551553
UniProtP0CG30|GSTT2_HUMAN Glutathione S-transferase theta-2B (Gene Name=GSTT2B)

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