Structure of PDB 2hnl Chain B

Receptor sequence
>2hnlB (length=200) Species: 6282 (Onchocerca volvulus) [Search protein sequence]
EKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFGHV
PMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELFQK
LIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNKVS
VADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKTYF
3D structure
PDB2hnl Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y32 R38 R43
Catalytic site (residue number reindexed from 1) Y7 R13 R18
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 Y32 R38 W63 K67 G73 H74 V75 E87 S88 Y7 R13 W38 K42 G48 H49 V50 E62 S63
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2hnl, PDBe:2hnl, PDBj:2hnl
PDBsum2hnl
PubMed18258257
UniProtP46434|GST1_ONCVO Glutathione S-transferase 1 (Fragment) (Gene Name=GST1)

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