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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2VEL
| 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: | 2-PHOSPHOGLYCOLIC ACID, CHLORIDE ION, 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: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (2.3 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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2V5F
| Crystal structure of wild type peptide-binding domain of human type I collagen prolyl 4-hydroxylase. | Descriptor: | HEXA-HISTIDINE PEPTIDE, PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1 | Authors: | Pekkala, M, Hieta, R, Kivirikko, K, Myllyharju, J, Wierenga, R. | Deposit date: | 2008-10-06 | Release date: | 2009-11-17 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.03 Å) | Cite: | Crystal Structure of Wild Type Peptide-Binding Domain of Human Type I Collagen Prolyl 4- Hydroxylase. To be Published
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2V2C
| The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-06-05 | Release date: | 2008-02-19 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (1.89 Å) | Cite: | Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim. Acta Crystallogr.,Sect.D, 64, 2008
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2VEI
| 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: | GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE, SULFATE ION | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.89 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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2VEK
| 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-(BUTYLSULPHONYL)-PROPANOIC ACID, CITRIC ACID, 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: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.6 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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2X58
| The crystal structure of MFE1 liganded with CoA | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, COENZYME A, GLYCEROL, ... | Authors: | Kasaragod, P, Venkatesan, R, Kiema, T.R, Hiltunen, J.K, Wierenga, R.K. | Deposit date: | 2010-02-05 | Release date: | 2010-05-12 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | The Crystal Structure of Liganded Rat Peroxisomal Multifunctional Enzyme Type 1: A Flexible Molecule with Two Interconnected Active Sites J.Biol.Chem., 285, 2010
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1N55
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2WL6
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1TJ7
| Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli | Descriptor: | Argininosuccinate lyase, GLYCEROL, PHOSPHATE ION | Authors: | Bhaumik, P, Koski, M.K, Bergman, U, Wierenga, R.K. | Deposit date: | 2004-06-03 | Release date: | 2004-10-26 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.44 Å) | Cite: | Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli. Acta Crystallogr.,Sect.D, 60, 2004
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1E15
| Chitinase B from Serratia Marcescens | Descriptor: | CHITINASE B | Authors: | Van Aalten, D.M.F, Synstad, B, Brurberg, M.B, Hough, E, Riise, B.W, Eijsink, V.G.H, Wierenga, R.K. | Deposit date: | 2000-04-18 | Release date: | 2000-08-18 | Last modified: | 2019-07-24 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure of a Two-Domain Chitotriosidase from Serratia Marcescens at 1.9 Angstrom Resoltuion Proc.Natl.Acad.Sci.USA, 97, 2000
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1TTI
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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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1SHF
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2V5L
| Structures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: as Observed in a New Crystal Form: Implications for the Reaction Mechanism | Descriptor: | SULFATE ION, TRIOSEPHOSPHATE ISOMERASE | Authors: | Noble, M.E.M, Zeelen, J.P, Wierenga, R.K. | Deposit date: | 2007-07-06 | Release date: | 2007-07-31 | Last modified: | 2024-05-08 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Structures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: As Observed in a New Crystal Form: Implications for the Reaction Mechanism Proteins: Struct.,Funct., Genet., 16, 1993
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1TMH
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1QFL
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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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1TRD
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1TRE
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2WKT
| BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316A MUTANT WITH COENZYME A. | Descriptor: | ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ... | Authors: | Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K. | Deposit date: | 2009-06-18 | Release date: | 2009-11-03 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2 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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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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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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