8JG3
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8JG2
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8GQM
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8GQK
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8GQI
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8GQJ
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8GQF
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8GQH
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8GQN
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8GQL
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8GQG
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8PF8
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-72 | Descriptor: | (2~{R})-3-bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boranyloxypropane-1,2-diol, GLYCEROL, Probable fatty oxidation protein FadB, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-06-15 | Release date: | 2024-01-24 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (2.23 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQM
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-10 | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, 6-[(6-azanyl-4-oxidanyl-naphthalen-2-yl)sulfonylamino]-4-oxidanyl-naphthalene-2-sulfonic acid, 6-azanyl-4-oxidanyl-naphthalene-2-sulfonic acid, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (3.2 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OPX
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Trehalose (Fragment-B-TRE) | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, Putative acyltransferase Rv0859, SULFATE ION, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-10 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.9 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQO
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-49 | Descriptor: | GLYCEROL, Probable fatty oxidation protein FadB, Putative acyltransferase Rv0859, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.6 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQT
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-91 | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, 4-bromanylbenzenesulfonic acid, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-28 | Method: | X-RAY DIFFRACTION (2.62 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OPU
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Sulfamethoxazole (Fragment-B-E1) | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, GLYCEROL, Putative acyltransferase Rv0859, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-10 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (3.04 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OPW
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Caffeine (Fragment-B-51) | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, CAFFEINE, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-10 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.52 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. Acta Crystallogr D Struct Biol, 80, 2024
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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 | Last modified: | 2024-08-14 | 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQS
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-83 | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, 4-phenylbenzenesulfonic acid, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.33 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQR
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-80 | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, 4-cyanobenzenesulfonic acid, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.4 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQV
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-109 | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, 4-nitrobenzenesulfonic acid, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.78 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQN
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-53 | Descriptor: | 1-benzyl-1H-pyrazole-4-carboxylic acid, 3-hydroxyacyl-CoA dehydrogenase, Putative acyltransferase Rv0859, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.2 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQP
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-76 | Descriptor: | 2-azanyl-5-sulfo-benzoic acid, 3-hydroxyacyl-CoA dehydrogenase, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-08-14 | Method: | X-RAY DIFFRACTION (2.18 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. Acta Crystallogr D Struct Biol, 80, 2024
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8OQL
| Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-1 | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, GLYCEROL, Hexafluorophosphate anion, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-04-12 | Release date: | 2024-01-24 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (2.7 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. Acta Crystallogr D Struct Biol, 80, 2024
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