Structure of PDB 4l5l Chain A

Receptor sequence
>4l5lA (length=217) Species: 79923 (Clonorchis sinensis) [Search protein sequence]
MAPVLGYWKIRGLAQPIRLLLEYVGDSYEEHSYGRCDGEKWQNDKHNLGL
ELPNLPYYKDGNFSLTQSLAILRYIADKHNMIGNTPVERAKISMIEGGLV
DLRAGVSRIAYQETFEQLKVPYLQQLPSTLRMWSQFLGNNSYLHGSTPTH
LDFMFYEALDVIRYLDPTSVEAFPNLMQFIHRIEALPNIKAFMESDRFIK
WPLNGWSAYFGGGDAPP
3D structure
PDB4l5l Crystal structures of 26kDa Clonorchis sinensis glutathione S-transferase reveal zinc binding and putative metal binding.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y7 L13
Catalytic site (residue number reindexed from 1) Y7 L13
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 W8 L13 W41 K45 N54 L55 Q67 S68 W8 L13 W41 K45 N54 L55 Q67 S68
BS02 ZN A D26 H79 D26 H79
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006749 glutathione metabolic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:4l5l, PDBe:4l5l, PDBj:4l5l
PDBsum4l5l
PubMed23916611
UniProtQ25595

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