Literature summary extracted from

Wang, W.C.; Hsu, W.H.; Chien, F.T.; Chen, C.Y.
Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft (2001), J. Mol. Biol., 306, 251-261.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.5.1.77	hanging-drop vapor-diffusion method, crystals belong to space group P2(1) with unit cell dimensions a = 70.23 A, b = 67.53 A, c = 137.48 A and beta = 96.12°. There are 4 molecules per asymmetric unit	Agrobacterium tumefaciens

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.5.1.77	H129A	inactive mutant enzyme	Agrobacterium tumefaciens
3.5.1.77	H129N	inactive mutant enzyme	Agrobacterium tumefaciens
3.5.1.77	H129R	inactive mutant enzyme	Agrobacterium tumefaciens
3.5.1.77	H144A	5% of the activity of wild-type enzyme	Agrobacterium tumefaciens
3.5.1.77	H215A	17% of the activity of wild-type enzyme	Agrobacterium tumefaciens

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.77	Agrobacterium tumefaciens	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.5.1.77	-	Agrobacterium tumefaciens

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Release 2023.1 (January 2023)