Structure of PDB 1ljr Chain A

Receptor sequence
>1ljrA (length=244) Species: 9606 (Homo sapiens) [Search protein sequence]
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINS
LGKLPTLKDGDFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLG
WHADCIRGTFGIPLWVQVLGPLIGVQVPEEKVERNRTAMDQALQWLEDKF
LGDRPFLAGQQVTLADLMALEELMQPVALGYELFEGRPRLAAWRGRVEAF
LGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRIARIP
3D structure
PDB1ljr Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.
ChainA
Resolution3.2 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 GSH A S11 P13 H40 K41 K53 L54 E66 S67 S11 P13 H40 K41 K53 L54 E66 S67
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:1ljr, PDBe:1ljr, PDBj:1ljr
PDBsum1ljr
PubMed9551553
UniProtP0CG30|GSTT2_HUMAN Glutathione S-transferase theta-2B (Gene Name=GSTT2B)

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