Structure of PDB 3erg Chain A

Receptor sequence
>3ergA (length=208) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MIIYDTPAGPYPARVRIALAEKNMLSSVQFVRINLWKGEHKKPEFLAKNY
SGTVPVLELDDGTLIAECTAITEYIDALDGTPTLTGKTPLEKGVIHMMNK
RAELELLDPVSVYFHHATPGLGPEVELYQNKEWGLRQRDKALHGMHYFDT
VLRERPYVAGDSFSMADITVIAGLIFAAIVKLQVPEECEALRAWYKRMQQ
RPSVKKLL
3D structure
PDB3erg Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G27
Catalytic site (residue number reindexed from 1) G9
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 GTS A P28 Y29 P30 H58 T71 V72 E85 C86 H133 P10 Y11 P12 H40 T53 V54 E67 C68 H115
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0043295 glutathione binding
Biological Process
GO:0006749 glutathione metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3erg, PDBe:3erg, PDBj:3erg
PDBsum3erg
PubMed19851333
UniProtQ12390|GST2_YEAST Glutathione S-transferase 2 (Gene Name=GTT2)

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