3AT1
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5AT1
| STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION | Descriptor: | ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, ... | Authors: | Stevens, R.C, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1990-04-26 | Release date: | 1990-10-15 | Last modified: | 2017-11-29 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. Biochemistry, 29, 1990
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6AT1
| STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION | Descriptor: | ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, ... | Authors: | Stevens, R.C, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1990-04-26 | Release date: | 1990-10-15 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. Biochemistry, 29, 1990
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7AT1
| CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H | Descriptor: | ADENOSINE-5'-TRIPHOSPHATE, ASPARTATE CARBAMOYLTRANSFERASE (R STATE), CATALYTIC CHAIN, ... | Authors: | Gouaux, J.E, Stevens, R.C, Lipscomb, W.N. | Deposit date: | 1989-09-22 | Release date: | 1990-10-15 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH. Biochemistry, 29, 1990
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1ACM
| ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY | Descriptor: | ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN, ... | Authors: | Stevens, R.C, Kantrowitz, E.R, Lipscomb, W.N. | Deposit date: | 1992-07-08 | Release date: | 1992-07-15 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study. Protein Sci., 1, 1992
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1AT1
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4AT1
| STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION | Descriptor: | ADENOSINE-5'-TRIPHOSPHATE, ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN, ... | Authors: | Stevens, R.C, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1990-04-26 | Release date: | 1990-10-15 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. Biochemistry, 29, 1990
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2AT1
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5HJ7
| Glutamate Racemase Mycobacterium tuberculosis (MurI) with bound D-glutamate, 2.3 Angstrom resolution, X-ray diffraction | Descriptor: | D-GLUTAMIC ACID, Glutamate racemase | Authors: | Poen, S, Nakatani, Y, Krause, K. | Deposit date: | 2016-01-12 | Release date: | 2016-05-25 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Exploring the structure of glutamate racemase from Mycobacterium tuberculosis as a template for anti-mycobacterial drug discovery. Biochem. J., 473, 2016
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6W6P
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6WUB
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6WUA
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6WU9
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6O90
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6O8Z
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6O8X
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6O8W
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6O8Y
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1VPR
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5UAU
| Structure of human PYCR-1 complexed with proline | Descriptor: | PROLINE, Pyrroline-5-carboxylate reductase 1, mitochondrial, ... | Authors: | Tanner, J.J. | Deposit date: | 2016-12-20 | Release date: | 2017-03-15 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. J. Biol. Chem., 292, 2017
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5UAV
| Structure of human PYCR-1 complexed with NADPH and L-tetrahydrofuroic acid | Descriptor: | DI(HYDROXYETHYL)ETHER, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, Pyrroline-5-carboxylate reductase 1, ... | Authors: | Tanner, J.J. | Deposit date: | 2016-12-20 | Release date: | 2017-03-15 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. J. Biol. Chem., 292, 2017
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5UAX
| Structure of apo human PYCR-1 crystallized in space group C2 | Descriptor: | CHLORIDE ION, Pyrroline-5-carboxylate reductase 1, mitochondrial | Authors: | Tanner, J.J. | Deposit date: | 2016-12-20 | Release date: | 2017-03-15 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. J. Biol. Chem., 292, 2017
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5UAW
| Structure of apo human PYCR-1 crystallized in space group P21212 | Descriptor: | Pyrroline-5-carboxylate reductase 1, mitochondrial, SULFATE ION | Authors: | Tanner, J.J. | Deposit date: | 2016-12-20 | Release date: | 2017-03-15 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. J. Biol. Chem., 292, 2017
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5UAT
| Structure of human PYCR-1 complexed with NADPH | Descriptor: | DI(HYDROXYETHYL)ETHER, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, Pyrroline-5-carboxylate reductase 1, ... | Authors: | Tanner, J.J. | Deposit date: | 2016-12-20 | Release date: | 2017-03-15 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.92 Å) | Cite: | Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. J. Biol. Chem., 292, 2017
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