1SPA
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1spa by Molmil](/molmil-images/mine/1spa) | ROLE OF ASP222 IN THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE: THE AMINO ACID RESIDUE WHICH ENHANCES THE FUNCTION OF THE ENZYME-BOUND COENZYME PYRIDOXAL 5'-PHOSPHATE | Descriptor: | ASPARTATE AMINOTRANSFERASE, N-METHYL-4-DEOXY-4-AMINO-PYRIDOXAL-5-PHOSPHATE | Authors: | Hinoue, Y, Yano, T, Metzler, D.E, Miyahara, I, Hirotsu, K, Kagamiyama, H. | Deposit date: | 1993-01-26 | Release date: | 1993-10-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate. Biochemistry, 31, 1992
|
|
2AY2
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay2 by Molmil](/molmil-images/mine/2ay2) | |
2AY7
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay7 by Molmil](/molmil-images/mine/2ay7) | |
2AY3
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay3 by Molmil](/molmil-images/mine/2ay3) | AROMATIC AMINO ACID AMINOTRANSFERASE WITH 3-(3,4-DIMETHOXYPHENYL)PROPIONIC ACID | Descriptor: | 3-(3,4-DIMETHOXYPHENYL)PROPIONIC ACID, AROMATIC AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Okamoto, A, Hirotsu, K, Kagamiyama, H. | Deposit date: | 1998-08-06 | Release date: | 1999-02-02 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity. Biochemistry, 38, 1999
|
|
2AY9
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay9 by Molmil](/molmil-images/mine/2ay9) | |
2AY8
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay8 by Molmil](/molmil-images/mine/2ay8) | |
2AY5
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay5 by Molmil](/molmil-images/mine/2ay5) | |
2AY6
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay6 by Molmil](/molmil-images/mine/2ay6) | |
2AY4
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay4 by Molmil](/molmil-images/mine/2ay4) | |
2AY1
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2ay1 by Molmil](/molmil-images/mine/2ay1) | |
1L6F
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1l6f by Molmil](/molmil-images/mine/1l6f) | Alanine racemase bound with N-(5'-phosphopyridoxyl)-L-alanine | Descriptor: | ALANYL-PYRIDOXAL-5'-PHOSPHATE, alanine racemase | Authors: | Watanabe, A, Yoshimura, T, Mikami, B, Hayashi, H, Kagamiyama, H, Esaki, N. | Deposit date: | 2002-03-09 | Release date: | 2002-06-05 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine. J.Biol.Chem., 277, 2002
|
|
1L6G
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1l6g by Molmil](/molmil-images/mine/1l6g) | Alanine racemase bound with N-(5'-phosphopyridoxyl)-D-alanine | Descriptor: | N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE, alanine racemase | Authors: | Watanabe, A, Yoshimura, T, Mikami, B, Hayashi, H, Kagamiyama, H, Esaki, N. | Deposit date: | 2002-03-10 | Release date: | 2002-06-05 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine. J.Biol.Chem., 277, 2002
|
|
1CZC
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1czc by Molmil](/molmil-images/mine/1czc) | ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH GLUTARIC ACID | Descriptor: | GLUTARIC ACID, PROTEIN (ASPARTATE AMINOTRANSFERASE), PYRIDOXAL-5'-PHOSPHATE | Authors: | Okamoto, A, Oue, S, Yano, T, Kagamiyama, H. | Deposit date: | 1999-09-02 | Release date: | 2000-02-28 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex. J.Biochem.(Tokyo), 127, 2000
|
|
1CZE
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1cze by Molmil](/molmil-images/mine/1cze) | ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH SUCCINIC ACID | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, SUCCINIC ACID | Authors: | Okamoto, A, Oue, S, Yano, T, Kagamiyama, H. | Deposit date: | 1999-09-02 | Release date: | 2000-02-28 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex. J.Biochem.(Tokyo), 127, 2000
|
|
1YOO
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1yoo by Molmil](/molmil-images/mine/1yoo) | ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID | Descriptor: | ASPARTATE AMINOTRANSFERASE, ISOVALERIC ACID, PYRIDOXAL-5'-PHOSPHATE | Authors: | Oue, S, Okamoto, A, Yano, T, Kagamiyama, H. | Deposit date: | 1998-06-26 | Release date: | 1999-02-02 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J.Biol.Chem., 274, 1999
|
|
1AY5
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1ay5 by Molmil](/molmil-images/mine/1ay5) | AROMATIC AMINO ACID AMINOTRANSFERASE COMPLEX WITH MALEATE | Descriptor: | AROMATIC AMINO ACID AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | Authors: | Okamoto, A, Hirotsu, K, Kagamiyama, H. | Deposit date: | 1997-11-14 | Release date: | 1998-10-14 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. J.Mol.Biol., 280, 1998
|
|
1AY4
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1ay4 by Molmil](/molmil-images/mine/1ay4) | AROMATIC AMINO ACID AMINOTRANSFERASE WITHOUT SUBSTRATE | Descriptor: | AROMATIC AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Okamoto, A, Hirotsu, K, Kagamiyama, H. | Deposit date: | 1997-11-14 | Release date: | 1998-10-14 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2.33 Å) | Cite: | Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. J.Mol.Biol., 280, 1998
|
|
1AY8
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1ay8 by Molmil](/molmil-images/mine/1ay8) | |
1G7W
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1g7w by Molmil](/molmil-images/mine/1g7w) | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/R386L | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Mizuguchi, H, Hayashi, H, Okada, K, Miyahara, I, Hirotsu, K, Kagamiyama, H. | Deposit date: | 2000-11-15 | Release date: | 2000-11-29 | Last modified: | 2021-10-27 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Biochemistry, 40, 2001
|
|
1G4V
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1g4v by Molmil](/molmil-images/mine/1g4v) | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/Y225F | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Mizuguchi, H, Hayashi, H, Okada, K, Miyahara, I, Hirotsu, K, Kagamiyama, H. | Deposit date: | 2000-10-28 | Release date: | 2000-11-22 | Last modified: | 2021-10-27 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Biochemistry, 40, 2001
|
|
1G7X
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1g7x by Molmil](/molmil-images/mine/1g7x) | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/R292L/R386L | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Mizuguchi, H, Hayashi, H, Okada, K, Miyahara, I, Hirotsu, K, Kagamiyama, H. | Deposit date: | 2000-11-15 | Release date: | 2000-11-29 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Biochemistry, 40, 2001
|
|
1AMS
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1ams by Molmil](/molmil-images/mine/1ams) | X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAMINE 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN THREE FORMS | Descriptor: | 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ASPARTATE AMINOTRANSFERASE, GLUTARIC ACID | Authors: | Miyahara, I, Hirotsu, K, Hayashi, H, Kagamiyama, H. | Deposit date: | 1994-07-01 | Release date: | 1994-09-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. J.Biochem.(Tokyo), 116, 1994
|
|
1A3G
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1a3g by Molmil](/molmil-images/mine/1a3g) | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI | Descriptor: | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Okada, K, Hirotsu, K, Sato, M, Hayashi, H, Kagamiyama, H. | Deposit date: | 1998-01-21 | Release date: | 1998-05-27 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution. J.Biochem.(Tokyo), 121, 1997
|
|
1AMR
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1amr by Molmil](/molmil-images/mine/1amr) | X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAMINE 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN THREE FORMS | Descriptor: | 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ASPARTATE AMINOTRANSFERASE, MALEIC ACID | Authors: | Miyahara, I, Hirotsu, K, Hayashi, H, Kagamiyama, H. | Deposit date: | 1994-07-01 | Release date: | 1994-09-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. J.Biochem.(Tokyo), 116, 1994
|
|
1AMQ
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 1amq by Molmil](/molmil-images/mine/1amq) | X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAMINE 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN THREE FORMS | Descriptor: | 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ASPARTATE AMINOTRANSFERASE | Authors: | Miyahara, I, Hirotsu, K, Hayashi, H, Kagamiyama, H. | Deposit date: | 1994-07-01 | Release date: | 1994-09-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. J.Biochem.(Tokyo), 116, 1994
|
|