TRIOSEPHOSPHATE ISOMERASE
Trypanosoma cruzi
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain A； UniProt 3–251 Chain B； UniProt 3–251 | Not recorded | No other associated polymer | X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；pH 7.5 | Resolution 1.83 Å R-free 0.258 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 1TCD | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1CI1 CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI IN HEXANE Deposited 1999-04-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
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 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
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 |
| 2OMA Crystallographic analysis of a chemically modified triosephosphate isomerase from Trypanosoma cruzi with dithiobenzylamine (DTBA) Deposited 2007-01-21 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
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 | Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
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 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
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 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
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 | Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
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 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
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 |
6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | TPIS_TRYCR |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–249； UniProt 3–251 Author chain B； PDBConstruct 1–249； UniProt 3–251 |
