1X28
 
 | | Crystal Structure of e.coli AspAT complexed with N-phosphopyridoxyl-L-glutamic acid | | Descriptor: | Aspartate aminotransferase, N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid | | Authors: | Goto, M. | | Deposit date: | 2005-04-21 | | Release date: | 2005-06-14 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step.
Biochemistry, 44, 2005
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1WRV
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1WLY
 | | Crystal Structure of 2-Haloacrylate Reductase | | Descriptor: | 2-haloacrylate reductase | | Authors: | Omi, R. | | Deposit date: | 2004-06-30 | | Release date: | 2005-10-04 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (1.3 Å) | | Cite: | Crystal Structure of 2-Haloacrylate Reductase
To be Published
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1X29
 | | Crystal Structure of e.coli AspAT complexed with N-phosphopyridoxyl-2-methyl-L-glutamic acid | | Descriptor: | Aspartate aminotransferase, N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-2-METHYL-L-GLUTAMIC ACID | | Authors: | Goto, M. | | Deposit date: | 2005-04-21 | | Release date: | 2005-06-14 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step.
Biochemistry, 44, 2005
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1Y37
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2YXZ
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2YXO
 | | Histidinol Phosphate Phosphatase complexed with Sulfate | | Descriptor: | FE (III) ION, GLYCEROL, Histidinol phosphatase, ... | | Authors: | Omi, R. | | Deposit date: | 2007-04-26 | | Release date: | 2007-11-27 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (1.6 Å) | | Cite: | Crystal Structure of Monofunctional Histidinol Phosphate Phosphatase from Thermus thermophilus HB8.
Biochemistry, 46, 2007
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2YZ5
 | | Histidinol Phosphate Phosphatase complexed with Phosphate | | Descriptor: | FE (III) ION, GLYCEROL, Histidinol phosphatase, ... | | Authors: | Omi, R. | | Deposit date: | 2007-05-03 | | Release date: | 2007-11-27 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Crystal Structure of Monofunctional Histidinol Phosphate Phosphatase from Thermus thermophilus HB8.
Biochemistry, 46, 2007
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3A9Z
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2ZR8
 | | Crystal Structure of Modified Serine Racemase complexed with Serine | | Descriptor: | MAGNESIUM ION, N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE, SERINE, ... | | Authors: | Goto, M. | | Deposit date: | 2008-08-25 | | Release date: | 2009-07-28 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe
J.Biol.Chem., 284, 2009
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3A9Y
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3A2B
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3A9X
 | | Crystal structure of rat selenocysteine lyase | | Descriptor: | PHOSPHATE ION, PYRIDOXAL-5'-PHOSPHATE, Selenocysteine lyase | | Authors: | Omi, R, Hirotsu, K. | | Deposit date: | 2009-11-08 | | Release date: | 2010-03-16 | | Last modified: | 2013-10-30 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
J.Biol.Chem., 285, 2010
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2Z4G
 | | Histidinol Phosphate Phosphatase from Thermus thermophilus HB8 | | Descriptor: | FE (III) ION, GLYCEROL, Histidinol phosphatase, ... | | Authors: | Omi, R. | | Deposit date: | 2007-06-17 | | Release date: | 2007-11-27 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Crystal Structure of Monofunctional Histidinol Phosphate Phosphatase from Thermus thermophilus HB8.
Biochemistry, 46, 2007
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2ZPU
 | | Crystal Structure of Modified Serine Racemase from S.pombe. | | Descriptor: | MAGNESIUM ION, N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE, Uncharacterized protein C320.14 | | Authors: | Goto, M. | | Deposit date: | 2008-07-29 | | Release date: | 2009-04-28 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (1.7 Å) | | Cite: | Serine racemase with catalytically active lysinoalanyl residue.
J.Biochem., 145, 2009
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2COI
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1IYD
 | | CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE | | Descriptor: | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE, GLUTARIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Hirotsu, K, Goto, M. | | Deposit date: | 2002-08-07 | | Release date: | 2003-05-06 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.15 Å) | | Cite: | Crystal structures of branched-chain amino Acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.
Biochemistry, 42, 2003
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2COG
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1J21
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1J1Z
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2DVX
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2DVT
 | | Crystal Structure of 2,6-Dihydroxybenzoate Decarboxylase from Rhizobium | | Descriptor: | Thermophilic reversible gamma-resorcylate decarboxylase, ZINC ION | | Authors: | Goto, M. | | Deposit date: | 2006-08-01 | | Release date: | 2006-09-19 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (1.7 Å) | | Cite: | Crystal Structures of Nonoxidative Zn-Dependent 2,6-Dihydroxybenzoate (gamma-Resorcylate) Decarboxylase
from Rhizobium sp. Strain MTP-10005
To be Published
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2COJ
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1G4X
 | | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/R292L | | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Mizuguchi, H. | | Deposit date: | 2000-10-29 | | Release date: | 2000-11-22 | | 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
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1IYE
 | | CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE | | Descriptor: | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE, N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid | | Authors: | Hirotsu, K, Goto, M. | | Deposit date: | 2002-08-07 | | Release date: | 2003-05-06 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (1.82 Å) | | Cite: | Crystal structures of branched-chain amino Acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.
Biochemistry, 42, 2003
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