8V9M
| Human Ornithine Aminotransferase cocrystallized with its inhibitor, (R)-3-amino-5,5-difluorocyclohex-1-ene-1-carboxylic acid. | Descriptor: | 3-fluoro-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]benzoic acid, GLYCEROL, Ornithine aminotransferase, ... | Authors: | Vargas, A.L, Devitt, A, Kaley, N, Silverman, R, Liu, D. | Deposit date: | 2023-12-08 | Release date: | 2024-05-08 | Last modified: | 2024-05-29 | Method: | X-RAY DIFFRACTION (1.61 Å) | Cite: | Design, Synthesis, and Mechanistic Studies of ( R )-3-Amino-5,5-difluorocyclohex-1-ene-1-carboxylic Acid as an Inactivator of Human Ornithine Aminotransferase. Acs Chem.Biol., 19, 2024
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2Z1Z
| Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana complexed with L-malate ion | Descriptor: | D-MALATE, LL-diaminopimelate aminotransferase, PYRIDOXAL-5'-PHOSPHATE | Authors: | Watanabe, N, Cherney, M.M, van Belkum, M.J, Marcus, S.L, Flegel, M.D, Clay, M.D, Deyholos, M.K, Vederas, J.C, James, M.N.G. | Deposit date: | 2007-05-16 | Release date: | 2007-07-17 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia J.Mol.Biol., 371, 2007
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2Z20
| Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana | Descriptor: | GLYCEROL, LL-diaminopimelate aminotransferase, PYRIDOXAL-5'-PHOSPHATE, ... | Authors: | Watanabe, N, Cherney, M.M, van Belkum, M.J, Marcus, S.L, Flegel, M.D, Clay, M.D, Deyholos, M.K, Vederas, J.C, James, M.N.G. | Deposit date: | 2007-05-17 | Release date: | 2007-07-17 | Last modified: | 2011-07-13 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia J.Mol.Biol., 371, 2007
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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
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2V3U
| Structure of the ligand-binding core of the ionotropic glutamate receptor-like GluRdelta2 in complex with D-serine | Descriptor: | CHLORIDE ION, D-SERINE, GLUTAMATE RECEPTOR DELTA-2 SUBUNIT, ... | Authors: | Naur, P, Vestergaard, B, Gajhede, M, Kastrup, J.S. | Deposit date: | 2007-06-22 | Release date: | 2007-08-07 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.74 Å) | Cite: | Ionotropic Glutamate-Like Receptor {Delta}2 Binds D-Serine and Glycine. Proc.Natl.Acad.Sci.USA, 104, 2007
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1BQA
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1BQD
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1B4X
| ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE | Descriptor: | ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | Authors: | Jeffery, C.J, Gloss, L.M, Petsko, G.A, Ringe, D. | Deposit date: | 1998-12-30 | Release date: | 2000-10-27 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2.45 Å) | Cite: | The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Eng., 13, 2000
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2HHF
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3R3L
| Structure of NP protein from Lassa AV strain | Descriptor: | MANGANESE (II) ION, Nucleoprotein, ZINC ION | Authors: | Perbandt, M, Brunotte, L, Gunther, S, Betzel, C. | Deposit date: | 2011-03-16 | Release date: | 2011-09-14 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (2.449 Å) | Cite: | Structure of the Lassa virus nucleoprotein revealed by X-ray crystallography, small-angle X-ray scattering, and electron microscopy. J.Biol.Chem., 286, 2011
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3DC1
| Crystal structure of kynurenine aminotransferase II complex with alpha-ketoglutarate | Descriptor: | 2-OXOGLUTARIC ACID, GLYCEROL, Kynurenine/alpha-aminoadipate aminotransferase mitochondrial | Authors: | Han, Q, Cai, T, Tagle, D.A, Robinson, H, Li, J. | Deposit date: | 2008-06-03 | Release date: | 2008-07-29 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II Biosci.Rep., 28, 2008
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2JDX
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1H1C
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2DAB
| L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE | Descriptor: | D-AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Sugio, S, Kashima, A, Kishimoto, K, Peisach, D, Petsko, G.A, Ringe, D, Yoshimura, T, Esaki, N. | Deposit date: | 1997-11-30 | Release date: | 1998-06-03 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination. Protein Eng., 11, 1998
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1AKB
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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
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1AKA
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1AKC
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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
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3RBS
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1ASM
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2EGY
| Crystal structure of LysN, alpha-aminoadipate aminotransferase (substrate free form), from Thermus thermophilus HB27 | Descriptor: | Alpha-aminodipate aminotransferase, PYRIDOXAL-5'-PHOSPHATE | Authors: | Tomita, T, Miyazaki, T, Miyagawa, T, Fushinobu, S, Kuzuyama, T, Nishiyama, M. | Deposit date: | 2007-03-02 | Release date: | 2008-03-04 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (2.67 Å) | Cite: | Crystal structure of LysN, alpha-aminoadipate aminotransferase, from Thermus thermophilus HB27 To be Published
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1ASN
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1ASL
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1IX6
| Aspartate Aminotransferase Active Site Mutant V39F | Descriptor: | Aspartate Aminotransferase, PYRIDOXAL-5'-PHOSPHATE | Authors: | Hayashi, H, Mizuguchi, H, Miyahara, I, Nakajima, Y, Hirotsu, K, Kagamiyama, H. | Deposit date: | 2002-06-14 | Release date: | 2002-07-03 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis J.BIOL.CHEM., 278, 2003
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