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1IIG
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STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE
分子名称: 3-PHOSPHONOPROPANOIC ACID, TRIOSEPHOSPHATE ISOMERASE
著者Noble, M.E, Wierenga, R.K, Lambeir, A.M, Opperdoes, F.R, Thunnissen, A.M, Kalk, K.H, Groendijk, H, Hol, W.G.J.
登録日2001-04-23
公開日2001-05-11
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.6 Å)
主引用文献The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Proteins, 10, 1991
1IIH
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STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE
分子名称: 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE
著者Noble, M.E, Wierenga, R.K, Lambeir, A.M, Opperdoes, F.R, Thunnissen, A.M, Kalk, K.H, Groendijk, H, Hol, W.G.J.
登録日2001-04-23
公開日2001-05-11
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.2 Å)
主引用文献The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Proteins, 10, 1991
1EVZ
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CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD
分子名称: GLYCEROL-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PENTADECANE
著者Suresh, S, Turley, S, Opperdoes, F.R, Michels, P.A.M, Hol, W.G.J.
登録日2000-04-21
公開日2001-02-22
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献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
1EVY
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BU of 1evy by Molmil
CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE
分子名称: GLYCEROL-3-PHOSPHATE DEHYDROGENASE, PENTADECANE
著者Suresh, S, Turley, S, Opperdoes, F.R, Michels, P.A.M, Hol, W.G.J.
登録日2000-04-20
公開日2001-02-22
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (1.75 Å)
主引用文献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
5TIM
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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
分子名称: 2,3-DIHYDROXY-1,4-DITHIOBUTANE, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE
著者Wierenga, R.K, Hol, W.G.J.
登録日1991-04-23
公開日1992-10-15
最終更新日2024-03-06
実験手法X-RAY DIFFRACTION (1.83 Å)
主引用文献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
6TIM
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THE ADAPTABILITY OF THE ACTIVE SITE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AS OBSERVED IN THE CRYSTAL STRUCTURES OF THREE DIFFERENT COMPLEXES
分子名称: SN-GLYCEROL-3-PHOSPHATE, TRIOSEPHOSPHATE ISOMERASE
著者Noble, M.E.M, Wierenga, R.K, Hol, W.G.J.
登録日1991-04-23
公開日1992-10-15
最終更新日2024-03-13
実験手法X-RAY DIFFRACTION (2.2 Å)
主引用文献The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Proteins, 10, 1991
1TSI
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STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO-BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP
分子名称: N-HYDROXY-4-PHOSPHONO-BUTANAMIDE, TRIOSEPHOSPHATE ISOMERASE
著者Verlinde, C.L.M.J.
登録日1992-11-19
公開日1994-01-31
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.84 Å)
主引用文献Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.
Protein Sci., 1, 1992
4TIM
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CRYSTALLOGRAPHIC AND MOLECULAR MODELING STUDIES ON TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: A CRITICAL ASSESSMENT OF THE PREDICTED AND OBSERVED STRUCTURES OF THE COMPLEX WITH 2-PHOSPHOGLYCERATE
分子名称: 2-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE
著者Nobel, M.E.M, Wierenga, R.K, Hol, W.G.J.
登録日1991-04-11
公開日1992-10-15
最終更新日2024-02-28
実験手法X-RAY DIFFRACTION (2.4 Å)
主引用文献Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate.
J.Med.Chem., 34, 1991
3TIM
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BU of 3tim by Molmil
THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE
分子名称: TRIOSEPHOSPHATE ISOMERASE
著者Wierenga, R.K.
登録日1990-05-15
公開日1991-10-15
最終更新日2024-02-28
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase.
Proteins, 10, 1991
2X0N
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Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data
分子名称: GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, GLYCOSOMAL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ...
著者Vellieux, F.M.D, Hajdu, J, Hol, W.G.J.
登録日2009-12-16
公開日2009-12-22
最終更新日2023-12-20
実験手法X-RAY DIFFRACTION (3.2 Å)
主引用文献Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma Brucei Determined from Laue Data.
Proc.Natl.Acad.Sci.USA, 90, 1993
1GYQ
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CRYSTAL STRUCTURE OF GLYCOSOMAL GLYCERALDEHYDE FROM LEISHMANIA MEXICANA IN COMPLEX WITH N6-BENZYL-NAD
分子名称: N6-BENZYL-NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PROTEIN (GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE)
著者Suresh, S, Hol, W.
登録日1999-03-05
公開日1999-03-16
最終更新日2023-08-09
実験手法X-RAY DIFFRACTION (3.4 Å)
主引用文献Structure-based design of submicromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase.
Proc.Natl.Acad.Sci.USA, 96, 1999
1AMK
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LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE
分子名称: 2-PHOSPHOGLYCOLIC ACID, TRIOSE PHOSPHATE ISOMERASE
著者Williams, J.C, Wierenga, R.
登録日1997-06-17
公開日1997-12-17
最終更新日2023-08-02
実験手法X-RAY DIFFRACTION (1.83 Å)
主引用文献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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