PDB Information

PDB5F05
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourcePopulus trichocarpa
Primary Citation
Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities.
Pegeot, H., Mathiot, S., Perrot, T., Gense, F., Hecker, A., Didierjean, C., Rouhier, N.
FEBS J.
HeaderTransferase
Released2015-11-27
Resolution1.700
CATH Insert Date25 Dec, 2016

PDB Images (13)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 26 Dec, 2016 Chopped
B 26 Dec, 2016 Chopped
C 26 Dec, 2016 Chopped
D 26 Dec, 2016 Chopped

CATH Domains (8)

Domain ID Date inserted into CATH Superfamily CATH Status
5f05A01 29 Dec, 2016 3.40.30.10 Assigned
5f05A02 29 Dec, 2016 1.20.1050.10 Assigned
5f05B01 29 Dec, 2016 3.40.30.10 Assigned
5f05B02 29 Dec, 2016 1.20.1050.10 Assigned
5f05C01 29 Dec, 2016 3.40.30.10 Assigned
5f05C02 29 Dec, 2016 1.20.1050.10 Assigned
5f05D01 29 Dec, 2016 3.40.30.10 Assigned
5f05D02 29 Dec, 2016 1.20.1050.10 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
D2WL63 D2WL63_POPTR Populus trichocarpa Phi class glutathione transferase GSTF5
D2WL63 D2WL63_POPTR Populus trichocarpa Phi class glutathione transferase GSTF5
D2WL63 D2WL63_POPTR Populus trichocarpa Phi class glutathione transferase GSTF5
D2WL63 D2WL63_POPTR Populus trichocarpa Phi class glutathione transferase GSTF5