2WL5
| BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348N MUTANT WITH COENZYME A. | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ... | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | Deposit date: | 2009-06-22 | Release date: | 2009-11-03 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation. Biochemistry, 48, 2009
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2WKV
| BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316D MUTANT WITH COENZYME A. | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, COENZYME A, SODIUM ION, ... | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | Deposit date: | 2009-06-18 | Release date: | 2009-11-03 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation. Biochemistry, 48, 2009
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2WKU
| BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT. | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, D-mannose, SULFATE ION | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | Deposit date: | 2009-06-18 | Release date: | 2009-11-03 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation. Biochemistry, 48, 2009
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2WL4
| BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348A MUTANT WITH COENZYME A. | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ... | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | Deposit date: | 2009-06-22 | Release date: | 2009-11-03 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation. Biochemistry, 48, 2009
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6TP5
| Crystal structure of human Transmembrane prolyl 4-hydroxylase | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, CHLORIDE ION, ... | Authors: | Myllykoski, M, Sutinen, A, Koski, M.K, Kallio, J.P, Raasakka, A, Myllyharju, J, Wierenga, R.K, Koivunen, P. | Deposit date: | 2019-12-12 | Release date: | 2020-12-23 | Last modified: | 2024-10-23 | Method: | X-RAY DIFFRACTION (2.25 Å) | Cite: | Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. J.Biol.Chem., 296, 2020
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1TTJ
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1AFW
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1AW2
| TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS | Descriptor: | SULFATE ION, TRIOSEPHOSPHATE ISOMERASE | Authors: | Maes, D, Zeelen, J.P, Wierenga, R.K. | Deposit date: | 1997-10-09 | Release date: | 1998-01-28 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (2.65 Å) | Cite: | Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. J.Biol.Chem., 273, 1998
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1B9B
| TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA | Descriptor: | PROTEIN (TRIOSEPHOSPHATE ISOMERASE), SULFATE ION | Authors: | Maes, D, Wierenga, R.K. | Deposit date: | 1999-02-09 | Release date: | 2000-01-01 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (2.85 Å) | Cite: | The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins, 37, 1999
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1AW1
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1CSK
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2IB9
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2IBY
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2IB8
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2IB7
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2IBU
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2IBW
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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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2J24
| The functional role of the conserved active site proline of triosephosphate isomerase | Descriptor: | TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | Authors: | Casteleijn, M.G, Alahuhta, M, Groebel, K, El-Sayed, I, Augustyns, K, Lambeir, A.M, Neubauer, P, Wierenga, R.K. | Deposit date: | 2006-08-16 | Release date: | 2007-01-02 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase. Biochemistry, 45, 2006
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2J27
| The functional role of the conserved active site proline of triosephosphate isomerase. | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | Authors: | Casteleijn, M.G, Alahuhta, M, Groebel, K, El-Sayed, I, Augustyns, K, Lambeir, A.M, Neubauer, P, Wierenga, R.K. | Deposit date: | 2006-08-16 | Release date: | 2007-01-02 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (1.15 Å) | Cite: | Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase. Biochemistry, 45, 2006
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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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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: | 2024-10-23 | 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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