2IB8
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1OU6
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1NL7
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1PXT
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2IBU
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2IBW
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2JIG
| Crystal structure of Chlamydomonas reinhardtii prolyl-4 hydroxylase type I complexed with zinc and pyridine-2,4-dicarboxylate | Descriptor: | GLYCEROL, PROLYL-4 HYDROXYLASE, PYRIDINE-2,4-DICARBOXYLIC ACID, ... | Authors: | Koski, M.K, Hieta, R, Bollner, C, Kivirikko, K.I, Myllyharju, J, Wierenga, R.K. | Deposit date: | 2007-06-28 | Release date: | 2007-10-30 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | The Active Site of an Algal Prolyl 4-Hydroxylase Has a Large Structural Plasticity. J.Biol.Chem., 282, 2007
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2JIJ
| Crystal structure of the apo form of Chlamydomonas reinhardtii prolyl- 4 hydroxylase type I | Descriptor: | CHLORIDE ION, PROLYL-4 HYDROXYLASE | Authors: | Koski, M.K, Hieta, R, Bollner, C, Kivirikko, K.I, Myllyharju, J, Wierenga, R.K. | Deposit date: | 2007-06-28 | Release date: | 2007-10-30 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | The Active Site of an Algal Prolyl 4-Hydroxylase Has a Large Structural Plasticity. J.Biol.Chem., 282, 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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1QFL
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2IB9
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2IBY
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2IB7
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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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1DM3
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1DLU
| UNLIGANDED BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, BIOSYNTHETIC THIOLASE, SULFATE ION | Authors: | Modis, Y, Wierenga, R.K. | Deposit date: | 1999-12-12 | Release date: | 2000-04-24 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.25 Å) | Cite: | Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase. J.Mol.Biol., 297, 2000
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1DLV
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1E2X
| FadR, fatty acid responsive transcription factor from E. coli | Descriptor: | FATTY ACID METABOLISM REGULATOR PROTEIN, SULFATE ION | Authors: | Van Aalten, D.M.F, Dirusso, C.C, Knudsen, J, Wierenga, R.K. | Deposit date: | 2000-05-30 | Release date: | 2000-12-03 | Last modified: | 2024-05-08 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystal Structure of Fadr, a Fatty Acid-Responsive Transcription Factor with a Novel Acyl Coenzyme A-Binding Fold Embo J., 19, 2000
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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, 3-hydroxyacyl-CoA dehydrogenase, GLYCEROL, ... | Authors: | Dalwani, S, Wierenga, R.K, Venkatesan, R. | Deposit date: | 2023-06-15 | Release date: | 2024-01-24 | 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 Biorxiv, 2024
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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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2V4A
| Crystal structure of the SeMet-labeled prolyl-4 hydroxylase (P4H) type I from green algae Chlamydomonas reinhardtii. | Descriptor: | CHLORIDE ION, DIMETHYL SULFOXIDE, GLYCEROL, ... | Authors: | Koski, M.K, Hieta, R, Bollner, C, Kivirikko, K.I, Myllyharju, J, Wierenga, R.K. | Deposit date: | 2007-06-28 | Release date: | 2007-10-30 | Last modified: | 2019-07-24 | Method: | X-RAY DIFFRACTION (1.93 Å) | Cite: | The Active Site of an Algal Prolyl 4-Hydroxylase Has a Large Structural Plasticity. J.Biol.Chem., 282, 2007
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2VEM
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties | Descriptor: | (3-bromo-2-oxo-propoxy)phosphonic acid, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE, TERTIARY-BUTYL ALCOHOL | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-25 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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2VEN
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties | Descriptor: | CITRIC ACID, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-25 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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