Structure of PDB 1oe8 Chain B

Receptor sequence
>1oe8B (length=205) Species: 6185 (Schistosoma haematobium) [Search protein sequence]
GDHIKVIYFNGRGRAESIRMTLVAAGVNYEDERISFQDWPKIKPTIPGGR
LPAVKITDNHGHVKWMVESLAIARYMAKKHHMMGGTEEEYYNVEKLIGQA
EDLEHEYYKTLMKPEEEKQKIIKEILNGKVPVLLDIICESLKASTGKLAV
GDKVTLADLVLIAVIDHVTDLDKEFLTGKYPEIHKHRENLLASSPRLAKY
LSDRA
3D structure
PDB1oe8 Crystal Structure of the 28 kDa Glutathione S-Transferase from Schistosoma Haematobium
ChainB
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) Y10 R16 R21
Catalytic site (residue number reindexed from 1) Y8 R14 R19
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 R16 W41 K45 R52 L53 E70 S71 R14 W39 K43 R50 L51 E68 S69 MOAD: Kd=9uM
PDBbind-CN: -logKd/Ki=5.52,Kd=3uM
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1oe8, PDBe:1oe8, PDBj:1oe8
PDBsum1oe8
PubMed12939136
UniProtP30114|GST28_SCHBO Glutathione S-transferase class-mu 28 kDa isozyme

[Back to BioLiP]