Literature summary for 2.6.1.52 extracted from

Mishra, V.; Kumar, A.; Ali, V.; Nozaki, T.; Zhang, K.Y.; Bhakuni, V.
Role of conserved active site tryptophan-101 in functional activity and stability of phosphoserine aminotransferase from an enteric human parasite (2012), Amino Acids, 43, 483-491.

Crystallization (Commentary)

Crystallization (Comment)	Organism
energy-minimized average simulated model. the enzyme exists as a homodimer and each subunit of the protein is composed of two domains, a large pyridoxal phosphate-binding domain and a C-terminal domain. The enzyme harbors two active sites present at the subunit interface. The indole ring of residue Trp101 stacks with the pyridine ring of pyridoxal 5'-phopsphate at the active site and distance between the two moieties is about 5 A	Entamoeba histolytica

Crystallization (Comment)

Organism

energy-minimized average simulated model. the enzyme exists as a homodimer and each subunit of the protein is composed of two domains, a large pyridoxal phosphate-binding domain and a C-terminal domain. The enzyme harbors two active sites present at the subunit interface. The indole ring of residue Trp101 stacks with the pyridine ring of pyridoxal 5'-phopsphate at the active site and distance between the two moieties is about 5 A

Entamoeba histolytica

Protein Variants

Protein Variants	Comment	Organism
W101A	about 5% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. In mutant W101A, there are no big fluctuations but the stacking interaction is lost due to side chain truncation	Entamoeba histolytica
W101F	about 70% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein	Entamoeba histolytica
W101H	about 20% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein	Entamoeba histolytica

Organism

Organism	UniProt	Comment	Textmining
Entamoeba histolytica	-	-	-