Current Protein Identity:P52270 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1CI1 CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI IN HEXANE Deposited 1999-04-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–251(251 aa)
Chain B 1–251(251 aa)
Not recorded HEX HEXANE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 7.5;PROTEIN WAS CRYSTALLIZED AT ROOM TEMPERATUTE BY VAPER DIFFUSION FROM 0.1 M NA HEPES PH7.5, 2%(V/V) PEG400 AND 2.0 M AMMONIUM SULFATE, THEN SOAKED IN ANHYDROUS N-HEXANE. , VAPOR DIFFUSION
Resolution 2.00 Å R-free 0.239
1SUX CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI AND 3-(2-benzothiazolylthio)-1-propanesulfonic acid Deposited 2004-03-26 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–251(251 aa)
Chain B 1–251(251 aa)
Not recorded SO4 SULFATE ION × 7 BTS 3-(2-BENZOTHIAZOLYLTHIO)-1-PROPANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;PEG 400, HEPES, ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.00 Å R-free 0.196
1TCD TRYPANOSOMA CRUZI TRIOSEPHOSPHATE ISOMERASE Deposited 1998-01-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 3–251(249 aa)
Chain B 3–251(249 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;pH 7.5
Resolution 1.83 Å R-free 0.258
2OMA Crystallographic analysis of a chemically modified triosephosphate isomerase from Trypanosoma cruzi with dithiobenzylamine (DTBA) Deposited 2007-01-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 2–251(250 aa)
Chain B 2–251(250 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 9 PEG DI(HYDROXYETHYL)ETHER × 3 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;291 K;5 MICROL OF THE PROTEIN SOLUTION WERE MIXED WITH 5 MICROL OF 2 % POLYETHYLENE GLYCOL 400, 0.1 M HEPES, 2.0M AMMONIUM SULFATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.50. CRYSTAL SOAKED IN DITHIOBENZYLAMINE
Resolution 2.15 Å R-free 0.250
2V5B The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi Deposited 2008-10-02 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–68(68 aa) Fragment:RESIDUES 1-68,84-251
Chain A 84–251(168 aa) Fragment:RESIDUES 1-68,84-251
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 7.5;282 K;CRYSTALS WERE GROWN AT 9 DEGREES. RESERVOIR SOLUTION OF 100 MM HEPES, PH 7.5, 10% PEG 6000, AND 5% 2-METHYL-2,4-PENTANEDIOL. THE CRYSTALS WERE CRYOPROTECTED BY ADDING PEG 400 30% TO THE RESERVOIR. THEY WERE IMMEDIATELY FROZEN IN LIQUID NITROGEN.
Resolution 2.00 Å R-free 0.257
2V5B The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi Deposited 2008-10-02 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–68(68 aa) Fragment:RESIDUES 1-68,84-251
Chain A 84–251(168 aa) Fragment:RESIDUES 1-68,84-251
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 7.5;282 K;CRYSTALS WERE GROWN AT 9 DEGREES. RESERVOIR SOLUTION OF 100 MM HEPES, PH 7.5, 10% PEG 6000, AND 5% 2-METHYL-2,4-PENTANEDIOL. THE CRYSTALS WERE CRYOPROTECTED BY ADDING PEG 400 30% TO THE RESERVOIR. THEY WERE IMMEDIATELY FROZEN IN LIQUID NITROGEN.
Resolution 2.00 Å R-free 0.257
3Q37 Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes. Deposited 2010-12-21 Assembly 1 Insufficient information Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 35–90(56 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Chain A 121–251(131 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Chain B 35–90(56 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Chain B 121–251(131 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7;278 K;0.2 Sodium malonate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K
Resolution 1.65 Å R-free 0.220
3Q37 Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes. Deposited 2010-12-21 Assembly 2 Insufficient information Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 35–90(56 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Chain C 121–251(131 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Chain D 35–90(56 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Chain D 121–251(131 aa) Fragment:UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7;278 K;0.2 Sodium malonate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K
Resolution 1.65 Å R-free 0.220
4HHP Crystal structure of triosephosphate isomerase from trypanosoma cruzi, mutant e105d Deposited 2012-10-10 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–251(251 aa)
Chain B 1–251(251 aa)
Mutation:E105D Mutation:E105D GOL GLYCEROL × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.6;281.15 K;25% w/v PEG monomethyl ether 2000, 0.1 M Tris pH 8.6, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K
Resolution 1.50 Å R-free 0.196