1AG1
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MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Verlinde, C.L.M.J., Hol, W.G.J.
Deposit date:1997-03-28
Release date:1997-06-16
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.36 Å)
Cite:Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.
Eur.J.Biochem., 198, 1991
1AMK
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LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE
Descriptor:TRIOSE PHOSPHATE ISOMERASE
Authors:Williams, J.C., Wierenga, R.
Deposit date:1997-06-17
Release date:1997-12-17
Last modified:2011-11-16
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
1AW1
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TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS COMPLEXED WITH 2-PHOSPHOGLYCOLATE
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Maes, D., Zeelen, J.P., Wierenga, R.K.
Deposit date:1997-10-09
Release date:1998-01-28
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.7 Å)
Cite:Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
J.Biol.Chem., 273, 1998
1AW2
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TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Maes, D., Zeelen, J.P., Wierenga, R.K.
Deposit date:1997-10-09
Release date:1998-01-28
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.65 Å)
Cite:Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
J.Biol.Chem., 273, 1998
1B9B
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TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA
Descriptor:TRIOSEPHOSPHATE ISOMERASE (E.C.5.3.1.1)
Authors:Maes, D., Wierenga, R.K.
Deposit date:1999-02-09
Release date:2000-01-01
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.85 Å)
Cite:The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
Proteins, 37, 1999
1BTM
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TRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Delboni, L.F., Mande, S.C., Hol, W.G.J.
Deposit date:1995-11-11
Release date:1996-04-03
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
Protein Sci., 4, 1995
1CI1
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CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI IN HEXANE
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Gao, X.-G., Maldondo, E., Perez-Montfort, R., De Gomez-Puyou, M.T., Gomez-Puyou, A., Rodriguez-Romero, A.
Deposit date:1999-04-06
Release date:1999-09-01
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane.
Proc.Natl.Acad.Sci.USA, 96, 1999
1HTI
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CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME
Descriptor:TRIOSEPHOSPHATE ISOMERASE (TIM) (E.C.5.3.1.1) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID
Authors:Mande, S.C., Hol, W.G.J.
Deposit date:1994-10-12
Release date:1995-01-26
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.
Protein Sci., 3, 1994
1I45
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YEAST TRIOSEPHOSPHATE ISOMERASE (MUTANT)
Descriptor:Triosephosphate Isomerase (E.C.5.3.1.1)
Authors:Rozovsky, S., Jogl, G., Tong, L., McDermott, A.E.
Deposit date:2001-02-19
Release date:2001-06-30
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
J.Mol.Biol., 310, 2001
1IF2
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X-RAY STRUCTURE OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH IPP
Descriptor:Triosephosphate isomerase (E.C.5.3.1.1)
Authors:Kursula, I., Partanen, S., Lambeir, A.-M., Antonov, D.M., Augustyns, K., Wierenga, R.K.
Deposit date:2001-04-12
Release date:2001-08-17
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:Structural determinants for ligand binding and catalysis of triosephosphate isomerase.
Eur.J.Biochem., 268, 2001
1IIG
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STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE
Descriptor:triosephosphate isomerase (E.C.5.3.1.1)
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:2009-02-24
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
1IIH
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STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE
Descriptor:triosephosphate isomerase (E.C.5.3.1.1)
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:2009-02-24
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
1KV5
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STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TIM WITH THE SALT-BRIDGE-FORMING RESIDUE ARG191 MUTATED TO SER
Descriptor:triosephosphate isomerase, glycosomal (E.C.5.3.1.1)
Authors:Kursula, I., Partanen, S., Lambeir, A.-M., Wierenga, R.K.
Deposit date:2002-01-25
Release date:2002-03-29
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
FEBS Lett., 518, 2002
1LYX
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PLASMODIUM FALCIPARUM TRIOSEPHOSPHATE ISOMERASE (PFTIM)-PHOSPHOGLYCOLATE COMPLEX
Descriptor:Triosephosphate Isomerase (E.C.5.3.1.1 )
Authors:Parthasarathy, S., Balaram, H., Balaram, P., Murthy, M.R.
Deposit date:2002-06-10
Release date:2003-01-28
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state
Biochemistry, 41, 2002
1LZO
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PLASMODIUM FALCIPARUM TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLATE COMPLEX
Descriptor:Triosephosphate Isomerase (E.C.5.3.1.1 )
Authors:Parthasarathy, S., Balaram, H., Balaram, P., Murthy, M.R.
Deposit date:2002-06-11
Release date:2003-01-28
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state
Biochemistry, 41, 2002
1M6J
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CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ENTAMOEBA HISTOLYTICA
Descriptor:Triosephosphate Isomerase (E.C.5.3.1.1)
Authors:Rodriguez-Romero, A., Hernandez-Santoyo, A., Fernandez-Velasco, D.A.
Deposit date:2002-07-16
Release date:2002-10-12
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Structure and Inactivation of Triosephosphate Isomerase from Entamoeba histolytica
J.Mol.Biol., 322, 2002
1M7O
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PLASMODIUM FALCIPARUM TRIOSEPHOSPHATE ISOMERASE (PFTIM) COMPLED TO SUBSTRATE ANALOG 3-PHOSPHOGLYCERATE (3PG)
Descriptor:Triosephosphate Isomerase (E.C.5.3.1.1 )
Authors:Parthasarathy, S., Balaram, H., Balaram, P., Murthy, M.R.N.
Deposit date:2002-07-22
Release date:2002-11-29
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.
Acta Crystallogr.,Sect.D, 58, 2002
1M7P
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PLASMODIUM FALCIPARUM TRIOSEPHOSPHATE ISOMERASE (PFTIM) COMPLED TO SUBSTRATE ANALOG GLYCEROL-3-PHOSPHATE (G3P).
Descriptor:Triosephosphate Isomerase (E.C.5.3.1.1 )
Authors:Parthasarathy, S., Balaram, H., Balaram, P., Murthy, M.R.N.
Deposit date:2002-07-22
Release date:2002-11-29
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.
Acta Crystallogr.,Sect.D, 58, 2002
1MO0
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STRUCTURAL GENOMICS OF CAENORHABDITIS ELEGANS: TRIOSE PHOSPHATE ISOMERASE
Descriptor:Triosephosphate isomerase (E.C.5.3.1.1)
Authors:Symersky, J., Li, S., Finley, J., Liu, Z.-J., Qui, H., Luan, C.H., Carson, M., Tsao, J., Johnson, D., Lin, G., Zhao, J., Thomas, W., Nagy, L.A., Sha, B., DeLucas, L.J., Wang, B.-C., Luo, M., Southeast Collaboratory for Structural Genomics (SECSG)
Deposit date:2002-09-06
Release date:2002-09-13
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structural genomics of Caenorhabditis elegans: triosephosphate isomerase
Proteins, 51, 2003
1N55
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0.83A RESOLUTION STRUCTURE OF THE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 2-PHOSPHOGLYCOLATE
Descriptor:Triosephosphate isomerase (E.C.5.3.1.1)
Authors:Kursula, I., Wierenga, R.K.
Deposit date:2002-11-04
Release date:2003-01-21
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (0.83 Å)
Cite:Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
J.Biol.Chem., 278, 2003
1NEY
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TRIOSEPHOSPHATE ISOMERASE IN COMPLEX WITH DHAP
Descriptor:triosephosphate isomerase (E.C.5.3.1.1)
Authors:Jogl, G., Rozovsky, S., McDermott, A.E., Tong, L.
Deposit date:2002-12-12
Release date:2003-01-07
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (1.2 Å)
Cite:Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Proc.Natl.Acad.Sci.USA, 100, 2003
1NF0
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TRIOSEPHOSPHATE ISOMERASE IN COMPLEX WITH DHAP
Descriptor:triosephosphate isomerase (E.C.5.3.1.1)
Authors:Jogl, G., Rozovsky, S., McDermott, A.E., Tong, L.
Deposit date:2002-12-12
Release date:2003-01-07
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution
Proc.Natl.Acad.Sci.USA, 100, 2003
1O5X
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PLASMODIUM FALCIPARUM TIM COMPLEXED TO 2-PHOSPHOGLYCERATE
Descriptor:Triosephosphate isomerase(E.C.5.3.1.1)
Authors:Parthasarathy, S., Eaazhisai, K., Balaram, H., Balaram, P., Murthy, M.R.
Deposit date:2003-10-06
Release date:2004-01-13
Last modified:2009-02-24
Method:X-RAY DIFFRACTION (1.1 Å)
Cite:Structure of Plasmodium falciparum Triose-phosphate Isomerase-2-Phosphoglycerate Complex at 1.1-A Resolution
J.Biol.Chem., 278, 2003
1QDS
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SUPERSTABLE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE (TIM)
Descriptor:TRIOSEPHOSPHATE ISOMERASE (5.3.1.1) MUTANT
Authors:Lambeir, A.M., Backmann, J., Ruiz-Sanz, J., Filimonov, V., Nielsen, J.E., Vriend, G., Kursula, I., Norledge, B.V., Wierenga, R.K.
Deposit date:1999-07-10
Release date:2000-12-13
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.
Eur.J.Biochem., 267, 2000
1R2R
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CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
Descriptor:Triosephosphate isomerase (E.C.5.3.1.1), DIMETHYL SULFOXIDE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
Authors:Aparicio, R., Ferreira, S.T., Polikarpov, I.
Deposit date:2003-09-29
Release date:2003-12-23
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
J.Mol.Biol., 334, 2003
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