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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2X1R
 | | Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | | Descriptor: | 3-(PROPYLSULFONYL)PROPANOIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, ... | | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | | Deposit date: | 2010-01-04 | | Release date: | 2010-01-26 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (1.98 Å) | | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
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2X2G
 | | CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE | | Descriptor: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | | Deposit date: | 2010-01-13 | | Release date: | 2010-01-26 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
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2X1U
 | | Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | | Descriptor: | SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | | Deposit date: | 2010-01-04 | | Release date: | 2010-01-26 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (1.84 Å) | | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
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2V2H
 | | 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, CHLORIDE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | | Deposit date: | 2007-06-06 | | Release date: | 2008-02-19 | | Last modified: | 2024-05-01 | | Method: | X-RAY DIFFRACTION (1.18 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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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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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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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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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: | 2024-10-16 | | 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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2V2D
 | | 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: | PHOSPHATE 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: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.3 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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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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2V0T
 | | 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: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | | Deposit date: | 2007-05-18 | | Release date: | 2008-02-19 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.2 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. D Biol. Crystallogr., 64, 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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2X16
 | | Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | | Descriptor: | TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | | Deposit date: | 2009-12-21 | | Release date: | 2009-12-29 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.13 Å) | | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
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2X1T
 | | Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | | Descriptor: | 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | | Deposit date: | 2010-01-04 | | Release date: | 2010-01-26 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (1.83 Å) | | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase
Acta Crystallogr.,Sect.D, 66, 2010
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