1IIG
| STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE | Descriptor: | 3-PHOSPHONOPROPANOIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Noble, M.E, Wierenga, R.K, Lambeir, A.M, Opperdoes, F.R, Thunnissen, A.M, Kalk, K.H, Groendijk, H, Hol, W.G.J. | Deposit date: | 2001-04-23 | Release date: | 2001-05-11 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins, 10, 1991
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1IIH
| STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE | Descriptor: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Noble, M.E, Wierenga, R.K, Lambeir, A.M, Opperdoes, F.R, Thunnissen, A.M, Kalk, K.H, Groendijk, H, Hol, W.G.J. | Deposit date: | 2001-04-23 | Release date: | 2001-05-11 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins, 10, 1991
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1EVZ
| CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD | Descriptor: | GLYCEROL-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PENTADECANE | Authors: | Suresh, S, Turley, S, Opperdoes, F.R, Michels, P.A.M, Hol, W.G.J. | Deposit date: | 2000-04-21 | Release date: | 2001-02-22 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure Fold.Des., 8, 2000
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1EVY
| CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE | Descriptor: | GLYCEROL-3-PHOSPHATE DEHYDROGENASE, PENTADECANE | Authors: | Suresh, S, Turley, S, Opperdoes, F.R, Michels, P.A.M, Hol, W.G.J. | Deposit date: | 2000-04-20 | Release date: | 2001-02-22 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.75 Å) | Cite: | A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure Fold.Des., 8, 2000
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6TIM
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5TIM
| REFINED 1.83 ANGSTROMS STRUCTURE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, CRYSTALLIZED IN THE PRESENCE OF 2.4 M-AMMONIUM SULPHATE. A COMPARISON WITH THE STRUCTURE OF THE TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE-GLYCEROL-3-PHOSPHATE COMPLEX | Descriptor: | 2,3-DIHYDROXY-1,4-DITHIOBUTANE, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE | Authors: | Wierenga, R.K, Hol, W.G.J. | Deposit date: | 1991-04-23 | Release date: | 1992-10-15 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (1.83 Å) | Cite: | Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex. J.Mol.Biol., 220, 1991
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4TIM
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1TSI
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3TIM
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2X0N
| Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data | Descriptor: | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, GLYCOSOMAL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | Authors: | Vellieux, F.M.D, Hajdu, J, Hol, W.G.J. | Deposit date: | 2009-12-16 | Release date: | 2009-12-22 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (3.2 Å) | Cite: | Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma Brucei Determined from Laue Data. Proc.Natl.Acad.Sci.USA, 90, 1993
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1GYQ
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1AMK
| LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, TRIOSE PHOSPHATE ISOMERASE | Authors: | Williams, J.C, Wierenga, R. | Deposit date: | 1997-06-17 | Release date: | 1997-12-17 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (1.83 Å) | Cite: | Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Eng., 12, 1999
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