Structure of PDB 2hnl Chain A

Receptor sequence
>2hnlA (length=202) Species: 6282 (Onchocerca volvulus) [Search protein sequence]
QMEKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFG
HVPMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELF
QKLIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNK
VSVADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKT
YF
3D structure
PDB2hnl Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus.
ChainA
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) Y9 R15 R20
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 R38 W63 K67 H74 V75 E87 S88 R15 W40 K44 H51 V52 E64 S65
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
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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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