1GYR
| Mutant form of enoyl thioester reductase from Candida tropicalis | Descriptor: | 2,4-DIENOYL-COA REDUCTASE, GLYCEROL, SULFATE ION | Authors: | Airenne, T.T, Torkko, J.M, Van Der Plas, S, Sormunen, R.T, Kastaniotis, A.J, Wierenga, R.K, Hiltunen, J.K. | Deposit date: | 2002-04-29 | Release date: | 2003-03-13 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Structure-Function Analysis of Enoyl Thioester Reductase Involved in Mitochondrial Maintenance J.Mol.Biol., 327, 2003
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1PJH
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1PN4
| Crystal structure of 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2 complexed with (3R)-hydroxydecanoyl-CoA. | Descriptor: | 1,2-ETHANEDIOL, 3R-HYDROXYDECANOYL-COENZYME A, Peroxisomal hydratase-dehydrogenase-epimerase | Authors: | Koski, M.K, Haapalainen, A.M, Hiltunen, J.K, Glumoff, T. | Deposit date: | 2003-06-12 | Release date: | 2004-04-13 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (2.35 Å) | Cite: | A Two-domain Structure of One Subunit Explains Unique Features of Eukaryotic Hydratase 2. J.Biol.Chem., 279, 2004
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1PN2
| Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2 | Descriptor: | 1,2-ETHANEDIOL, Peroxisomal hydratase-dehydrogenase-epimerase | Authors: | Koski, M.K, Haapalainen, A.M, Hiltunen, J.K, Glumoff, T. | Deposit date: | 2003-06-12 | Release date: | 2004-04-13 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | A Two-domain Structure of One Subunit Explains Unique Features of Eukaryotic Hydratase 2. J.Biol.Chem., 279, 2004
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1N9G
| Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis | Descriptor: | 2,4-dienoyl-CoA reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION | Authors: | Torkko, J.M, Koivuranta, K.T, Kastaniotis, A.J, Airenne, T.T, Glumoff, T, Ilves, M, Hartig, A, Gurvitz, A, Hiltunen, J.K. | Deposit date: | 2002-11-25 | Release date: | 2003-12-09 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.98 Å) | Cite: | Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers. J.Biol.Chem., 278, 2003
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2DUB
| ENOYL-COA HYDRATASE COMPLEXED WITH OCTANOYL-COA | Descriptor: | 2-ENOYL-COA HYDRATASE, OCTANOYL-COENZYME A | Authors: | Engel, C.K, Wierenga, R.K. | Deposit date: | 1997-04-28 | Release date: | 1998-04-29 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule. J.Mol.Biol., 275, 1998
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6Z5F
| CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH 3-KETODECANOYL-COA AND OXIDISED NICOTINAMIDE ADENINE DINUCLEOTIDE | Descriptor: | 3-KETO-DECANOYL-COA, GLYCEROL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | Authors: | Wierenga, R.K, Sridhar, S, Kiema, T.R. | Deposit date: | 2020-05-26 | Release date: | 2020-12-09 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (2.25 Å) | Cite: | Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallogr D Struct Biol, 76, 2020
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1DUB
| 2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5 | Descriptor: | 2-ENOYL-COA HYDRATASE, ACETOACETYL-COENZYME A | Authors: | Wierenga, R.K, Engel, C.K. | Deposit date: | 1996-06-10 | Release date: | 1997-07-07 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket. EMBO J., 15, 1996
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7AYC
| Crystal Structure of human mitochondrial 2-Enoyl Thioester Reductase (MECR) with single mutation G165Q | Descriptor: | CHLORIDE ION, Enoyl-[acyl-carrier-protein] reductase, mitochondrial | Authors: | Rahman, M.T, Koski, M.K, Autio, K.J, Kastaniotis, A.J, Wierenga, R.K, Hiltunen, J.K. | Deposit date: | 2020-11-12 | Release date: | 2022-06-01 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.02 Å) | Cite: | An engineered variant of MECR reductase reveals indispensability of long-chain acyl-ACPs for mitochondrial respiration. Nat Commun, 14, 2023
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7AYB
| Crystal Structure of wild type human mitochondrial 2-Enoyl Thioester Reductase (MECR) | Descriptor: | ACETIC ACID, CHLORIDE ION, Enoyl-[acyl-carrier-protein] reductase, ... | Authors: | Rahman, M.T, Koski, M.K, Autio, K.J, Kastaniotis, A.J, Wierenga, R.K, Hiltunen, J.K. | Deposit date: | 2020-11-12 | Release date: | 2022-06-01 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | An engineered variant of MECR reductase reveals indispensability of long-chain acyl-ACPs for mitochondrial respiration. Nat Commun, 14, 2023
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6Z5V
| CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH 3-KETODECANOYL-COA IN CROTONASE FOLD AND OXIDISED NICOTINAMIDE ADENINE DINUCLEOTIDE IN HAD FOLD | Descriptor: | 3-KETO-DECANOYL-COA, GLYCEROL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | Authors: | Wierenga, R.K, Sridhar, S, Kiema, T.R. | Deposit date: | 2020-05-27 | Release date: | 2020-12-09 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (2.33 Å) | Cite: | Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallogr D Struct Biol, 76, 2020
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6Z5O
| CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH COENZYME-A AND OXIDISED NICOTINAMIDE ADENINE DINUCLEOTIDE | Descriptor: | COENZYME A, GLYCEROL, NICOTINAMIDE, ... | Authors: | Wierenga, R.K, Sridhar, S, Kiema, T.R. | Deposit date: | 2020-05-27 | Release date: | 2020-12-09 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallogr D Struct Biol, 76, 2020
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2VCY
| Crystal Structure of 2-Enoyl Thioester Reductase of Human FAS II | Descriptor: | SULFATE ION, TRANS-2-ENOYL-COA REDUCTASE | Authors: | Haapalainen, A.M, Pudas, R, Smart, O.S, Wierenga, R.K. | Deposit date: | 2007-09-28 | Release date: | 2008-06-03 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.41 Å) | Cite: | Structural Enzymological Studies of 2-Enoyl Thioester Reductase of the Human Mitochondrial Fas II Pathway: New Insights Into its Substrate Recognition Properties. J.Mol.Biol., 379, 2008
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1IKT
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2GD0
| The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety | Descriptor: | (S)-2-METHYLMYRISTOYL-COENZYME A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR | Authors: | Bhaumik, P, Wierenga, R.K. | Deposit date: | 2006-03-15 | Release date: | 2007-02-20 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface J.Mol.Biol., 367, 2007
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2GD6
| The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety | Descriptor: | ACETYL COENZYME *A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR | Authors: | Bhaumik, P, Wierenga, R.K. | Deposit date: | 2006-03-15 | Release date: | 2007-02-20 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface J.Mol.Biol., 367, 2007
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2GCE
| The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety | Descriptor: | (R)-IBUPROFENOYL-COENZYME A, (S)-IBUPROFENOYL-COENZYME A, probable alpha-methylacyl-CoA racemase MCR | Authors: | Bhaumik, P, Wierenga, R.K. | Deposit date: | 2006-03-14 | Release date: | 2007-02-20 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface J.Mol.Biol., 367, 2007
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2GCI
| The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety | Descriptor: | (R)-2-METHYLMYRISTOYL-COENZYME A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR | Authors: | Bhaumik, P, Wierenga, R.K. | Deposit date: | 2006-03-14 | Release date: | 2007-02-20 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface J.Mol.Biol., 367, 2007
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2GD2
| The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety | Descriptor: | ACETOACETYL-COENZYME A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR | Authors: | Bhaumik, P, Wierenga, R.K. | Deposit date: | 2006-03-15 | Release date: | 2007-02-20 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface J.Mol.Biol., 367, 2007
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