Structure of PDB 4mpg Chain B

Receptor sequence
>4mpgB (length=252) Species: 9606 (Homo sapiens) [Search protein sequence]
DLGTEFQSMGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKS
KEFLQINSLGKLPTLKDGDFILTESSAILIYLSCKYQTPDHWYPSDLQAR
ARVHEYLGWHADCIRGTFGIPLWVQVLGPLIGVQVPKEKVERNRTAMDQA
LQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALGYELFEGRPRLAA
WRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRIAR
IP
3D structure
PDB4mpg Crystal Structure of Human Glutathione S-Transferase Theta-2 (Target EFI-507257)
ChainB
Resolution1.951 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S11 S14 I48 N49
Catalytic site (residue number reindexed from 1) S19 S22 I56 N57
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 B S11 P13 H40 K41 K53 L54 E66 S67 R107 S19 P21 H48 K49 K61 L62 E74 S75 R115
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4mpg, PDBe:4mpg, PDBj:4mpg
PDBsum4mpg
PubMed
UniProtP0CG30|GSTT2_HUMAN Glutathione S-transferase theta-2B (Gene Name=GSTT2B)

[Back to BioLiP]