Structure of PDB 5f05 Chain A

Receptor sequence
>5f05A (length=210) Species: 3694 (Populus trichocarpa) [Search protein sequence]
PLKLHGSVLSTNTQRVLATLYEKEVEFELVNVNLGAGEHKQEPHISLNPF
GQVPAAVDGDLKLFESRAISQYVAHQYASKGTQLGAAGNGYATILVWQEV
ESHQFDPSASKLVWEQVFKPVFGLPTDAALVAETEVTLGKVLDVYEARLS
QSKYLASDSFTLADLHHLPNIQALLGTPSKKLFDSRPHVSAWVASITGRP
AWGKVLALLP
3D structure
PDB5f05 Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities.
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
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 S12 N14 H41 K42 Q54 V55 E67 S68 S10 N12 H39 K40 Q52 V53 E65 S66
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0043295 glutathione binding
GO:0046872 metal ion 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:5f05, PDBe:5f05, PDBj:5f05
PDBsum5f05
PubMed28622459
UniProtD2WL63

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