1JSW
| NATIVE L-ASPARTATE AMMONIA LYASE | Descriptor: | ACETATE ION, L-ASPARTATE AMMONIA-LYASE, beta-D-glucopyranose | Authors: | Shi, W, Dunbar, J, Farber, G.K. | Deposit date: | 1997-02-19 | Release date: | 1997-06-16 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | The structure of L-aspartate ammonia-lyase from Escherichia coli. Biochemistry, 36, 1997
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1KT8
| HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL): THREE DIMENSIONAL STRUCTURE OF ENZYME IN ITS KETIMINE FORM WITH THE SUBSTRATE L-ISOLEUCINE | Descriptor: | ACETIC ACID, BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE, MITOCHONDRIAL, ... | Authors: | Yennawar, N.H, Conway, M.E, Yennawar, H.P, Farber, G.K, Hutson, S.M. | Deposit date: | 2002-01-15 | Release date: | 2002-11-20 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms Biochemistry, 41, 2002
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1KTA
| HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE : THREE DIMENSIONAL STRUCTURE OF THE ENZYME IN ITS PYRIDOXAMINE PHOSPHATE FORM. | Descriptor: | 3-METHYL-2-OXOBUTANOIC ACID, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ACETIC ACID, ... | Authors: | Yennawar, N.H, Conway, M.E, Yennawar, H.P, Farber, G.K, Hutson, S.M. | Deposit date: | 2002-01-15 | Release date: | 2002-11-20 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms Biochemistry, 41, 2002
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1QKK
| Crystal structure of the receiver domain and linker region of DctD from Sinorhizobium meliloti | Descriptor: | C4-DICARBOXYLATE TRANSPORT TRANSCRIPTIONAL REGULATORY PROTEIN | Authors: | Meyer, M.G, Park, S, Zeringue, L, Staley, M, Mckinstry, M, Kaufman, R.I, Zhang, H, Yan, D, Yennawar, N, Farber, G.K, Nixon, B.T. | Deposit date: | 1999-07-23 | Release date: | 2000-07-30 | Last modified: | 2024-05-08 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD. Faseb J., 15, 2001
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1SBH
| SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) MUTANT (M50F, N76D, G169A, Q206C, N218S, K256Y) | Descriptor: | CALCIUM ION, SUBTILISIN 8397+1 | Authors: | Kidd, R.D, Farber, G.K. | Deposit date: | 1995-09-01 | Release date: | 1995-12-07 | Last modified: | 2021-11-03 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | A weak calcium binding site in subtilisin BPN' has a dramatic effect on protein stability. J.Am.Chem.Soc., 118, 1996
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1SBI
| SUBTILISIN BPN' 8397 (E.C. 3.4.21.14) MUTANT (M50F, N76D, G169A, Q206C, N218S) | Descriptor: | CALCIUM ION, SUBTILISIN 8397 | Authors: | Kidd, R.D, Yennawar, H.P, Farber, G.K. | Deposit date: | 1995-09-01 | Release date: | 1995-12-07 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | A weak calcium binding site in subtilisin BPN' has a dramatic effect on protein stability. J.Am.Chem.Soc., 118, 1996
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1RBX
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1RBW
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1GHB
| A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN | Descriptor: | ACETYL GROUP, GAMMA-CHYMOTRYPSIN, HEXANE, ... | Authors: | Yennawar, H.P, Yennawar, N.H, Farber, G.K. | Deposit date: | 1994-04-06 | Release date: | 1994-06-22 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | A STRUCTURAL EXPLANATION FOR ENZYME MEMORY IN NONAQUEOUS SOLVENTS. J.Am.Chem.Soc., 117, 1995
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1GHA
| A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN | Descriptor: | GAMMA-CHYMOTRYPSIN A, ISOPROPYL ALCOHOL, PRO GLY VAL TYR PEPTIDE, ... | Authors: | Yennawar, H.P, Yennawar, N.H, Farber, G.K. | Deposit date: | 1994-04-06 | Release date: | 1994-06-22 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | A STRUCTURAL EXPLANATION FOR ENZYME MEMORY IN NONAQUEOUS SOLVENTS. J.Am.Chem.Soc., 117, 1995
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1YJB
| SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 35% DIMETHYLFORMAMIDE | Descriptor: | CALCIUM ION, SUBTILISIN 8397+1 | Authors: | Kidd, R.D, Farber, G.K. | Deposit date: | 1996-01-16 | Release date: | 1996-07-11 | Last modified: | 2021-11-03 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Breaking the low barrier hydrogen bond in a serine protease. Protein Sci., 8, 1999
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1YJA
| SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 20% DIMETHYLFORMAMIDE | Descriptor: | CALCIUM ION, SUBTILISIN 8397+1 | Authors: | Kidd, R.D, Farber, G.K. | Deposit date: | 1996-01-16 | Release date: | 1996-07-11 | Last modified: | 2021-11-03 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Breaking the low barrier hydrogen bond in a serine protease. Protein Sci., 8, 1999
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1YJC
| SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 50% DIMETHYLFORMAMIDE | Descriptor: | CALCIUM ION, SUBTILISIN 8397+1 | Authors: | Kidd, R.D, Farber, G.K. | Deposit date: | 1996-01-16 | Release date: | 1996-07-11 | Last modified: | 2021-11-03 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Breaking the low barrier hydrogen bond in a serine protease. Protein Sci., 8, 1999
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1DDS
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1DDR
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1GMD
| X-ray crystal structure of gamma-chymotrypsin in hexane | Descriptor: | GAMMA-CHYMOTRYPSIN A, HEXANE, PRO GLY ALA TYR ASP PEPTIDE | Authors: | Yennawar, N.H, Yennawar, H.P, Banerjee, S, Farber, G.K. | Deposit date: | 1993-08-20 | Release date: | 1993-10-31 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | X-ray crystal structure of gamma-chymotrypsin in hexane. Biochemistry, 33, 1994
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1GMC
| THE X-RAY CRYSTAL STRUCTURE OF THE TETRAHEDRAL INTERMEDIATE OF GAMMA-CHYMOTRYPSIN IN HEXANE | Descriptor: | GAMMA-CHYMOTRYPSIN A, PRO GLY ALA TYR PEPTIDE | Authors: | Yennawar, N.H, Yennawar, H.P, Banerjee, S, Farber, G.K. | Deposit date: | 1993-08-20 | Release date: | 1993-10-31 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | X-ray crystal structure of gamma-chymotrypsin in hexane. Biochemistry, 33, 1994
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2GYI
| DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A POTENT XYLOSE ISOMERASE INHIBITOR, D-THREONOHYDROXAMIC ACID, AND HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHIC STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX | Descriptor: | 2,3,4,N-TETRAHYDROXY-BUTYRIMIDIC ACID, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | Deposit date: | 1994-09-01 | Release date: | 1995-07-10 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Design, Synthesis, and Characterization of a Potent Xylose Isomerase Inhibitor, D-Threonohydroxamic Acid, and High-Resolution X-Ray Crystallographic Structure of the Enzyme-Inhibitor Complex Biochemistry, 34, 1995
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1XYM
| THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID | Descriptor: | D-glucose, HYDROXIDE ION, MAGNESIUM ION, ... | Authors: | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | Deposit date: | 1993-12-07 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Biochemistry, 33, 1994
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1XYA
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | Descriptor: | HYDROXIDE ION, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | Deposit date: | 1994-01-03 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.81 Å) | Cite: | X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry, 33, 1994
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1XYL
| THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID | Descriptor: | HYDROXIDE ION, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | Deposit date: | 1993-12-07 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Biochemistry, 33, 1994
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1XYC
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | Descriptor: | 3-O-METHYLFRUCTOSE IN LINEAR FORM, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | Deposit date: | 1994-01-03 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.19 Å) | Cite: | X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry, 33, 1994
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1XYB
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | Descriptor: | D-glucose, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | Deposit date: | 1994-01-03 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.96 Å) | Cite: | X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry, 33, 1994
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1EKF
| CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM) | Descriptor: | BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL), PYRIDOXAL-5'-PHOSPHATE | Authors: | Yennawar, N.H, Dunbar, J.H, Conway, M, Hutson, S.M, Farber, G.K. | Deposit date: | 2000-03-08 | Release date: | 2001-03-08 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr.,Sect.D, 57, 2001
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1EKP
| CRYSTAL STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 2.5 ANGSTROMS (MONOCLINIC FORM). | Descriptor: | BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL), PYRIDOXAL-5'-PHOSPHATE | Authors: | Yennawar, N.H, Dunbar, J.H, Conway, M, Hutson, S.M, Farber, G.K. | Deposit date: | 2000-03-09 | Release date: | 2001-03-09 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr.,Sect.D, 57, 2001
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