1TPF
| |
1TTI
| |
1TRI
| |
1TPV
| S96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASE | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Stock, A.M, Narayana, N, Xuong, Ng.H, Knowles, J.R, Petsko, G.A, Ringe, D. | Deposit date: | 1994-11-07 | Release date: | 1995-04-20 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase. Biochemistry, 35, 1996
|
|
1TPH
| 1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D. | Deposit date: | 1993-12-22 | Release date: | 1994-04-30 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. Biochemistry, 33, 1994
|
|
1TPW
| TRIOSEPHOSPHATE ISOMERASE DRINKS WATER TO KEEP HEALTHY | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Stock, A.M, Narayana, N, Xuong, Ng.H, Knowles, J.R, Petsko, G.A, Ringe, D. | Deposit date: | 1994-11-07 | Release date: | 1995-04-20 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | The role of water in the catalytic efficiency of triosephosphate isomerase. Biochemistry, 38, 1999
|
|
1TSI
| |
1TPC
| OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D. | Deposit date: | 1994-02-03 | Release date: | 1995-02-14 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules. Biochemistry, 34, 1995
|
|
1TPU
| S96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASE | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Stock, A.M, Narayana, N, Xuong, Ng.H, Knowles, J.R, Petsko, G.A, Ringe, D. | Deposit date: | 1994-11-07 | Release date: | 1995-04-20 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase. Biochemistry, 35, 1996
|
|
1W0M
| Triosephosphate isomerase from Thermoproteus tenax | Descriptor: | PHOSPHATE ION, TRIOSEPHOSPHATE ISOMERASE | Authors: | Walden, H, Taylor, G, Lorentzen, E, Pohl, E, Lilie, H, Schramm, A, Knura, T, Stubbe, K, Tjaden, B, Hensel, R. | Deposit date: | 2004-06-08 | Release date: | 2004-09-09 | Last modified: | 2019-07-24 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature J.Mol.Biol., 342, 2004
|
|
1VGA
| Structures of unligated and inhibitor complexes of W168F mutant of Triosephosphate Isomerase from Plasmodium falciparum | Descriptor: | Triosephosphate isomerase | Authors: | Eaazhisai, K, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2004-04-23 | Release date: | 2004-10-26 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6 J.Mol.Biol., 343, 2004
|
|
1WOB
| Structure of a loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase, W168F, complexed to sulfate | Descriptor: | SULFATE ION, Triosephosphate isomerase | Authors: | Eaazhisai, K, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2004-08-12 | Release date: | 2004-10-26 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6 J.Mol.Biol., 343, 2004
|
|
1WOA
| Structure of the loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase, W168F, complexed with Glycerol-2-phosphate | Descriptor: | 2-HYDROXY-1-(HYDROXYMETHYL)ETHYL DIHYDROGEN PHOSPHATE, Triosephosphate isomerase | Authors: | Eaazhisai, K, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2004-08-12 | Release date: | 2004-10-26 | Last modified: | 2023-10-25 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6 J.Mol.Biol., 343, 2004
|
|
1WYI
| human triosephosphate isomerase of new crystal form | Descriptor: | Triosephosphate isomerase | Authors: | Kinoshita, T. | Deposit date: | 2005-02-14 | Release date: | 2005-04-12 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method. Acta Crystallogr.,Sect.F, 61, 2005
|
|
2VFH
| Crystal structure of the F96W mutant of Plasmodium falciparum triosephosphate isomerase complexed with 3-phosphoglycerate | Descriptor: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2007-11-04 | Release date: | 2008-12-09 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site. Acta Crystallogr.,Sect.D, 65, 2009
|
|
2VFI
| Crystal structure of the Plasmodium falciparum triosephosphate isomerase in the loop closed state with 3-phosphoglycerate bound at the active site and interface | Descriptor: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2007-11-04 | Release date: | 2008-12-09 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.25 Å) | Cite: | Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site. Acta Crystallogr.,Sect.D, 65, 2009
|
|
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
|
|
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
|
|
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: | 2018-04-04 | 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
|
|
2VFE
| Crystal structure of F96S mutant of Plasmodium falciparum triosephosphate isomerase with 3- phosphoglycerate bound at the dimer interface | Descriptor: | 3-PHOSPHOGLYCERIC ACID, GLYCEROL, TRIOSEPHOSPHATE ISOMERASE | Authors: | Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2007-11-03 | Release date: | 2008-12-09 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site. Acta Crystallogr.,Sect.D, 65, 2009
|
|
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
|
|
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: | 2023-12-13 | 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
|
|
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
|
|
2V5B
| |
2VFF
| Crystal structure of the F96H mutant of Plasmodium falciparum triosephosphate isomerase | Descriptor: | TRIOSEPHOSPHATE ISOMERASE | Authors: | Gayathri, P, Banerjee, M, Vijayalakshmi, A, Balaram, H, Balaram, P, Murthy, M.R.N. | Deposit date: | 2007-11-04 | Release date: | 2008-12-09 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Biochemical and Structural Characterization of Residue 96 Mutants of Plasmodium Falciparum Triosephosphate Isomerase: Active-Site Loop Conformation, Hydration and Identification of a Dimer-Interface Ligand-Binding Site. Acta Crystallogr.,Sect.D, 65, 2009
|
|