|
137
|
382
|
1bkgA |
Aspartate aminotransferase from thermus thermophilus with maleate |
|
127
|
396
|
1asaA |
The structural basis for the reduced activity of the y226f(y225f) active site mutant of e. coli aspartate aminotransferase |
|
139
|
396
|
1argA |
Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex |
|
138
|
396
|
1arsA |
X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from escherichia coli in open and closed form |
|
133
|
396
|
1asnA |
Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms |
|
127
|
396
|
1asbA |
The structural basis for the reduced activity of the d223a(d222a) active site mutant of e. coli aspartate aminotransferase |
|
132
|
382
|
1bjwA |
Aspartate aminotransferase from thermus thermophilus |
|
131
|
396
|
1aseA |
The structure of wild type e. coli aspartate aminotransferase reconstituted with plp-n-oxide |
|
130
|
396
|
1asgA |
The structural basis for the reduced activity of the y226f(y225f) active site mutant of e. coli aspartate aminotransferase |
|
122
|
396
|
1ascA |
The structural basis for the reduced activity of the d223a(d222a) active site mutant of e. coli aspartate aminotransferase |
|
135
|
382
|
1b5oA |
Thermus thermophilus aspartate aminotransferase single mutant 1 |
|
142
|
396
|
1arhA |
Aspartate aminotransferase, y225r/r386a mutant |
|
116
|
396
|
1asfA |
The structural basis for the reduced activity of the y226f(y225f) active site mutant of e. coli aspartate aminotransferase |
|
137
|
382
|
1b5pA |
Thermus thermophilus aspartate aminotransferase double mutant 1 |
|
146
|
401
|
1akcA |
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking its pyridoxal-5'-phosphate-binding lysine residue |
|
149
|
401
|
1akaA |
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking its pyridoxal-5'-phosphate-binding lysine residue |
|
129
|
396
|
1amqA |
X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from escherichia coli in three forms |
|
148
|
412
|
1ajsB |
Refinement and comparison of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate |
|
140
|
401
|
1amaA |
Domain closure in mitochondrial aspartate aminotransferase |
|
147
|
412
|
1ajsA |
Refinement and comparison of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate |
|
140
|
396
|
1amrA |
X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from escherichia coli in three forms |
|
137
|
396
|
1amsA |
X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from escherichia coli in three forms |
|
143
|
412
|
1ajrA |
Refinement and comparison of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate |
|
149
|
401
|
1akbA |
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking its pyridoxal-5'-phosphate-binding lysine residue |
|
135
|
396
|
1ahxA |
Aspartate aminotransferase hexamutant |
|
130
|
396
|
1ahfA |
Aspartate aminotransferase hexamutant |
|
134
|
396
|
1aibA |
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate binding lysine residue |
|
122
|
396
|
1aawA |
The structural basis for the altered substrate specificity of the r292d active site mutant of aspartate aminotransferase from e. coli |
|
134
|
396
|
1aiaA |
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate binding lysine residue |
|
133
|
396
|
1aheA |
Aspartate aminotransferase hexamutant |
|
140
|
396
|
1aicA |
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate binding lysine residue |
|
69
|
396
|
1aamA |
The structural basis for the altered substrate specificity of the r292d active site mutant of aspartate aminotransferase from e. coli |
|
130
|
396
|
1ahyA |
Aspartate aminotransferase hexamutant |
|
125
|
396
|
1ahgA |
Aspartate aminotransferase hexamutant |
