6ARL
| Aspergillus fumigatus Cytosolic Thiolase: Apo enzyme in complex with rubidium ions | Descriptor: | Acetyl-CoA acetyltransferase, CHLORIDE ION, GLYCEROL, ... | Authors: | Marshall, A.C, Bond, C.S, Bruning, J.B. | Deposit date: | 2017-08-22 | Release date: | 2018-05-30 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations Acs Catalysis, 8(3), 2018
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6AQP
| Aspergillus fumigatus Cytosolic Thiolase: Acetylated enzyme in complex with CoA and potassium ions | Descriptor: | ACETYL COENZYME *A, Acetyl-CoA acetyltransferase, CHLORIDE ION, ... | Authors: | Marshall, A.C, Bond, C.S, Bruning, J.B. | Deposit date: | 2017-08-21 | Release date: | 2018-05-30 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations Acs Catalysis, 8(3), 2018
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6BJ9
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6BJA
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6BJB
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6BN2
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6DV2
| Crystal Structure of Human Mitochondrial Trifunctional Protein | Descriptor: | Trifunctional enzyme subunit alpha, mitochondrial, Trifunctional enzyme subunit beta | Authors: | Fu, Z, Xia, C, Battaile, K.P, Kim, J.P. | Deposit date: | 2018-06-22 | Release date: | 2018-09-26 | Last modified: | 2023-10-11 | Method: | X-RAY DIFFRACTION (3.6 Å) | Cite: | Crystal structure of human mitochondrial trifunctional protein, a fatty acid beta-oxidation metabolon. Proc. Natl. Acad. Sci. U.S.A., 116, 2019
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8K1C
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8JG2
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8JG3
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8OQL
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8OPW
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8OPX
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8OPV
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8OQN
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8OQV
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8OQQ
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8OQT
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8OPU
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8OQM
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8OQS
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8OQU
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8OQO
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8OQP
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8OPY
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-B-DNQ | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, 6,7-DINITROQUINOXALINE-2,3-DIONE, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-10 | Release date: | 2024-01-24 | Method: | X-RAY DIFFRACTION (2.45 Å) | Cite: | Crystallographic fragment binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate channeling path between them Biorxiv, 2024
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