Structure of PDB 1dug Chain A

Receptor sequence
>1dugA (length=234) Species: 6182,9606 [Search protein sequence]
SPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLE
FPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLD
IRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHP
DFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAW
PLQGWQATFGGGDHPPKSDPQQHHLGGAKQAGDV
3D structure
PDB1dug Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y6 L12
Catalytic site (residue number reindexed from 1) Y6 L12
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 W7 L12 W40 K44 N53 L54 Q66 S67 W7 L12 W40 K44 N53 L54 Q66 S67
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:1dug, PDBe:1dug, PDBj:1dug
PDBsum1dug
PubMed10631982
UniProtP02679|FIBG_HUMAN Fibrinogen gamma chain (Gene Name=FGG);
P08515|GST26_SCHJA Glutathione S-transferase class-mu 26 kDa isozyme

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