Structure of PDB 5f06 Chain B

Receptor sequence
>5f06B (length=213) Species: 3694 (Populus trichocarpa) [Search protein sequence]
VLKLYGAPMSTCTSRVLTCLHEKNLDFELVPVDLFAGEHKQPPFLAKNPF
GQIPALEEDDLTLFESRAITSYIAEKFKGTGYDLIRHENLKEAASVKVWT
EVESHRYNPAIAPIVFQFMVAPLRGNSPDQTIIDDNVEKLGKVLDIYEAK
LSSTKYLAGDFYSLADLHHLPYTYYLMKTPAASVVNERPHVKAWWEDISS
RPAFKKVAEGMNF
3D structure
PDB5f06 Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M10
Catalytic site (residue number reindexed from 1) M9
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 C13 L35 H40 Q53 I54 E66 S67 C12 L34 H39 Q52 I53 E65 S66
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0043295 glutathione binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0009407 toxin catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5f06, PDBe:5f06, PDBj:5f06
PDBsum5f06
PubMed28622459
UniProtU5GTL0

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