Structure of PDB 5lkd Chain B

Receptor sequence
>5lkdB (length=338) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
QVSSFRETISKQHPIYKPAKGRYWLYVSLACPWAHRTLITRALKGLTSVI
GCSVVHWHLDEKGWRFLDLEHWHDVAGGIRTASFAEIKNDSQRFMVDATN
EPHYGYKRISDLYYKSDPQYSARFTVPVLWDLETQTIVNNESSEIIRILN
SSAFDEFVDDDHKKTDLVPAQLKTQIDDFNSWVYDSINNGVYKTGFAEKA
EVYESEVNNVFEHLDKVEKILSDKYSKLKAKYGEEDRQKILGEFFTVGDQ
LTEADIRLYTTVIRFDPVYVQHFKCNFTSIRAGYPFIHLWVRNLYWNYDA
FRYTTDFDHIKLHYTRSHTRINPLGITPLGPKPDIRPL
3D structure
PDB5lkd Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.
ChainB
Resolution1.68 Å
3D
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
Enzyme Commision number 1.8.5.1: glutathione dehydrogenase (ascorbate).
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 C46 W48 W79 R155 T157 V158 E173 S174 C31 W33 W64 R123 T125 V126 E141 S142
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016491 oxidoreductase activity
GO:0016740 transferase activity
GO:0045174 glutathione dehydrogenase (ascorbate) activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0071555 cell wall organization
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5lkd, PDBe:5lkd, PDBj:5lkd
PDBsum5lkd
PubMed27736955
UniProtP36156|GTO2_YEAST Glutathione S-transferase omega-like 2 (Gene Name=ECM4)

[Back to BioLiP]