5LKR
| Human Butyrylcholinesterase complexed with N-Propargyliperidines | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Cholinesterase, ... | Authors: | Coquelle, N, Knez, D, Colletier, J.P, Gobec, S. | Deposit date: | 2016-07-23 | Release date: | 2016-12-14 | Last modified: | 2020-07-29 | Method: | X-RAY DIFFRACTION (2.52 Å) | Cite: | N-Propargylpiperidines with naphthalene-2-carboxamide or naphthalene-2-sulfonamide moieties: Potential multifunctional anti-Alzheimer's agents. Bioorg. Med. Chem., 25, 2017
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6SAM
| Structure of human butyrylcholinesterase in complex with 1-(2,3-dihydro-1H-inden2-yl)piperidin-3-yl N-phenyl carbamate | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, Cholinesterase, ... | Authors: | Brazzolotto, X, Kosak, U, Strasek, N, Knez, D, Gobec, S, Nachon, F. | Deposit date: | 2019-07-17 | Release date: | 2020-04-29 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | N-alkylpiperidine carbamates as potential anti-Alzheimer's agents. Eur.J.Med.Chem., 197, 2020
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3G49
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4K30
| Structure of the N-acetyltransferase domain of human N-acetylglutamate synthase | Descriptor: | N-ACETYL-L-GLUTAMATE, N-acetylglutamate synthase, mitochondrial | Authors: | Shi, D, Zhao, G, Jin, Z, Allewell, N.M, Tuchman, M. | Deposit date: | 2013-04-10 | Release date: | 2013-08-14 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (2.103 Å) | Cite: | Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms. Plos One, 8, 2013
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3M4J
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-11 | Release date: | 2010-07-28 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Reversible Post-Translational Carboxylation Modulates the Enzymatic Activity of N-Acetyl-l-ornithine Transcarbamylase. Biochemistry, 49, 2010
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3M4N
| Crystal structure of N-acetyl-L-ornithine transcarbamylase K302A mutant complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-11 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry, 49, 2010
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3M5D
| Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-12 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry, 49, 2010
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3M5C
| Crystal structure of N-acetyl-L-ornithine transcarbamylase K302E mutant complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-12 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry, 49, 2010
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2PRJ
| Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B | Descriptor: | GLYCOGEN PHOSPHORYLASE, INOSINIC ACID, N-acetyl-beta-D-glucopyranosylamine, ... | Authors: | Oikonomakos, N.G, Kontou, M, Zographos, S.E, Watson, K.A, Johnson, L.N, Bichard, C.J.F, Fleet, G.W.J, Acharya, K.R. | Deposit date: | 1998-12-11 | Release date: | 1998-12-16 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | N-acetyl-beta-D-glucopyranosylamine: a potent T-state inhibitor of glycogen phosphorylase. A comparison with alpha-D-glucose. Protein Sci., 4, 1995
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2FG7
| N-succinyl-L-ornithine transcarbamylase from B. fragilis complexed with carbamoyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, SULFATE ION, ... | Authors: | Shi, D, Yu, X, Malamy, M.H, Allewell, N.M, Tuchman, M. | Deposit date: | 2005-12-21 | Release date: | 2006-05-23 | Last modified: | 2023-11-29 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis. J.Biol.Chem., 281, 2006
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2FG6
| N-succinyl-L-ornithine transcarbamylase from B. fragilis complexed with sulfate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, SULFATE ION, putative ornithine carbamoyltransferase | Authors: | Shi, D, Yu, X, Malamy, M.H, Allewell, N.M, Mendel, T. | Deposit date: | 2005-12-21 | Release date: | 2006-05-23 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis. J.Biol.Chem., 281, 2006
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7XTM
| Crystal structure of the C-terminal domain of Bombyx mori N-acetylglucosaminyltransferase IV | Descriptor: | 1,2-ETHANEDIOL, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, N-acetylglucosaminyltransferase IV | Authors: | Miyazaki, T, Oka, N, Mori, S. | Deposit date: | 2022-05-17 | Release date: | 2022-09-28 | Last modified: | 2022-12-07 | Method: | X-RAY DIFFRACTION (1.47 Å) | Cite: | Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family. Glycobiology, 32, 2022
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7XTN
| Crystal structure of the C-terminal domain of Bombyx mori N-acetylglucosaminyltransferase IV in complex with N-acetylglucosamine | Descriptor: | 1,2-ETHANEDIOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, N-acetylglucosaminyltransferase IV | Authors: | Miyazaki, T, Oka, N, Mori, S. | Deposit date: | 2022-05-17 | Release date: | 2022-09-28 | Last modified: | 2022-12-07 | Method: | X-RAY DIFFRACTION (1.15 Å) | Cite: | Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family. Glycobiology, 32, 2022
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5D1J
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4C7F
| Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) | Descriptor: | 1,2-ETHANEDIOL, 6-ACETAMIDO-6-DEOXY-CASTANOSPERMINE, BETA-N-ACETYLHEXOSAMINIDASE | Authors: | Nguyen Thi, N, Offen, W.A, Davies, G.J, Doucet, N. | Deposit date: | 2013-09-20 | Release date: | 2014-03-12 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure and Activity of the Streptomyces Coelicolor A3(2) Beta-N-Acetylhexosaminidase Provides Further Insight Into Gh20 Family Catalysis and Inhibition. Biochemistry, 53, 2014
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4C7G
| Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) | Descriptor: | 1,2-ETHANEDIOL, 2-METHYL-4,5-DIHYDRO-(1,2-DIDEOXY-ALPHA-D-GLUCOPYRANOSO)[2,1-D]-1,3-OXAZOLE, BETA-N-ACETYLHEXOSAMINIDASE | Authors: | Nguyenthi, N, Offen, W.A, Davies, G.J, Doucet, N. | Deposit date: | 2013-09-20 | Release date: | 2014-03-12 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure and Activity of the Streptomyces Coelicolor A3(2) Beta-N-Acetylhexosaminidase Provides Further Insight Into Gh20 Family Catalysis and Inhibition. Biochemistry, 53, 2014
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2V0I
| Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU) | Descriptor: | BIFUNCTIONAL PROTEIN GLMU, DI(HYDROXYETHYL)ETHER, SULFATE ION, ... | Authors: | Mochalkin, I, Lightle, S, Ohren, J.F, Chirgadze, N.Y. | Deposit date: | 2007-05-14 | Release date: | 2008-01-15 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.89 Å) | Cite: | Characterization of Substrate Binding and Catalysis in the Potential Antibacterial Target N-Acetylglucosamine-1-Phosphate Uridyltransferase (Glmu). Protein Sci., 16, 2007
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4A32
| CRYSTAL STRUCTURE OF LEISHMANIA MAJOR N-MYRISTOYLTRANSFERASE (NMT) WITH BOUND MYRISTOYL-COA AND A PYRAZOLE SULPHONAMIDE LIGAND | Descriptor: | 3,5-DICHLORO-3'-[(DIETHYLAMINO)METHYL]-N-(1,3,5-TRIMETHYL-1H-PYRAZOL-4-YL)BIPHENYL-4-SULFONAMIDE, GLYCEROL, GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, ... | Authors: | Robinson, D.A, Brand, S, Cleghorn, L.A.T, McElroy, S.P, Smith, V.C, Hallyburton, I, Harrison, J.R, Norcross, N.R, Norval, S, Spinks, D, Stojanovski, L, Torrie, L.S, Frearson, J.A, Brenk, R, Fairlamb, A.H, Ferguson, M.A.J, Read, K.D, Wyatt, P.G, Gilbert, I.H. | Deposit date: | 2011-09-29 | Release date: | 2011-12-21 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Discovery of a novel class of orally active trypanocidal N-myristoyltransferase inhibitors. J. Med. Chem., 55, 2012
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4A33
| CRYSTAL STRUCTURE OF LEISHMANIA MAJOR N-MYRISTOYLTRANSFERASE (NMT) WITH BOUND MYRISTOYL-COA AND A PYRAZOLE SULPHONAMIDE LIGAND | Descriptor: | 2,6-DICHLORO-4-(6-PIPERAZIN-1-YLPYRIDIN-3-YL)-N-(1,3,5-TRIMETHYL-1H-PYRAZOL-4-YL)BENZENESULFONAMIDE, GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, TETRADECANOYL-COA | Authors: | Robinson, D.A, Brand, S, Cleghorn, L.A.T, McElroy, S.P, Smith, V.C, Hallyburton, I, Harrison, J.R, Norcross, N.R, Norval, S, Spinks, D, Stojanovski, L, Torrie, L.S, Frearson, J.A, Brenk, R, Fairlamb, A.H, Ferguson, M.A.J, Read, K.D, Wyatt, P.G, Gilbert, I.H. | Deposit date: | 2011-09-29 | Release date: | 2011-12-21 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Discovery of a novel class of orally active trypanocidal N-myristoyltransferase inhibitors. J. Med. Chem., 55, 2012
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4A31
| CRYSTAL STRUCTURE OF LEISHMANIA MAJOR N-MYRISTOYLTRANSFERASE (NMT) WITH BOUND MYRISTOYL-COA AND A PYRAZOLE SULPHONAMIDE LIGAND | Descriptor: | 6-{[2-(4-METHYLPIPERAZIN-1-YL)ETHYL]AMINO}-N-(1,3,5-TRIMETHYL-1H-PYRAZOL-4-YL)PYRIDINE-3-SULFONAMIDE, GLYCEROL, GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, ... | Authors: | Robinson, D.A, Brand, S, Cleghorn, L.A.T, McElroy, S.P, Smith, V.C, Hallyburton, I, Harrison, J.R, Norcross, N.R, Norval, S, Spinks, D, Stojanovski, L, Torrie, L.S, Frearson, J.A, Brenk, R, Fairlamb, A.H, Ferguson, M.A.J, Read, K.D, Wyatt, P.G, Gilbert, I.H. | Deposit date: | 2011-09-29 | Release date: | 2011-12-21 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (2.09 Å) | Cite: | Discovery of a novel class of orally active trypanocidal N-myristoyltransferase inhibitors. J. Med. Chem., 55, 2012
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3L02
| Crystal structure of N-acetyl-L-ornithine transcarbamylase E92A mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-09 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Protein Sci., 16, 2007
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3L04
| Crystal structure of N-acetyl-L-ornithine transcarbamylase E92P mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-09 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Protein Sci., 16, 2007
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3KZO
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline | Descriptor: | GLYCEROL, N-ACETYL-L-NORVALINE, N-acetylornithine carbamoyltransferase, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64, 2006
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3L06
| Crystal structure of N-acetyl-L-ornithine transcarbamylase E92V mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-09 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.81 Å) | Cite: | A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Protein Sci., 16, 2007
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3KZN
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with N-acetyl-L-ornirthine | Descriptor: | GLYCEROL, N-acetylornithine carbamoyltransferase, N~2~-ACETYL-L-ORNITHINE, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64, 2006
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