Current Protein Identity:P60174 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
1HTI CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME Deposited 1994-10-12 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–248(248 aa)
Chain B 1–248(248 aa)
Not recorded PGA 2-PHOSPHOGLYCOLIC ACID × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å
1WYI human triosephosphate isomerase of new crystal form Deposited 2005-02-14 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–248(248 aa)
Chain B 1–248(248 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions gel-tube under microgavity;pH 8;293 K;PEG4000, MgCl2, pH 8.0, gel-tube under microgavity, temperature 293K
Resolution 2.20 Å R-free 0.296
1WYI human triosephosphate isomerase of new crystal form Deposited 2005-02-14 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–248(248 aa)
Chain B 1–248(248 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions gel-tube under microgavity;pH 8;293 K;PEG4000, MgCl2, pH 8.0, gel-tube under microgavity, temperature 293K
Resolution 2.20 Å R-free 0.296
2IAM Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR Deposited 2006-09-08 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain P 22–36(15 aa) Fragment:residues 23-37 (22-36)
Mutation:T28I No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;8% PEG6000, 0.1M di-ammonium phosphate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.80 Å R-free 0.279
2IAN Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR Deposited 2006-09-08 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain C 22–36(15 aa) Fragment:residues 23-37 (22-36)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;10% PEG6000, 0.1M di-ammonium phosphate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.80 Å R-free 0.296
2IAN Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR Deposited 2006-09-08 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain H 22–36(15 aa) Fragment:residues 23-37 (22-36)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;10% PEG6000, 0.1M di-ammonium phosphate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.80 Å R-free 0.296
2IAN Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR Deposited 2006-09-08 Assembly 3 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain M 22–36(15 aa) Fragment:residues 23-37 (22-36)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;10% PEG6000, 0.1M di-ammonium phosphate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.80 Å R-free 0.296
2IAN Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR Deposited 2006-09-08 Assembly 4 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain R 22–36(15 aa) Fragment:residues 23-37 (22-36)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;10% PEG6000, 0.1M di-ammonium phosphate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.80 Å R-free 0.296
2JK2 STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. CRYSTAL STRUCTURE OF THE WILD TYPE ENZYME. Deposited 2008-06-22 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 2–249(248 aa) Fragment:RESIDUES 2-249
Chain B 2–249(248 aa) Fragment:RESIDUES 2-249
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;100 MM TRIS PH 8.5, 20% PEG MME2000, 10 MM NICL2
Resolution 1.70 Å R-free 0.252
2VOM Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation. Deposited 2008-02-19 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 2–249(248 aa) Fragment:RESIDUES 2-249
Chain B 2–249(248 aa) Fragment:RESIDUES 2-249
Mutation:YES Mutation:YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;100 MM TRIS PH 8.5, 20% PEG MME2000, 4% POLYPROPYLENE GLYCOL P400, 10 MM NICL2
Resolution 1.85 Å R-free 0.253
2VOM Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation. Deposited 2008-02-19 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 2–249(248 aa) Fragment:RESIDUES 2-249
Chain D 2–249(248 aa) Fragment:RESIDUES 2-249
Mutation:YES Mutation:YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;100 MM TRIS PH 8.5, 20% PEG MME2000, 4% POLYPROPYLENE GLYCOL P400, 10 MM NICL2
Resolution 1.85 Å R-free 0.253
4BR1 Protease-induced heterodimer of human triosephosphate isomerase. Deposited 2013-06-03 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 41–286(246 aa)
Chain B 41–286(246 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;100 MM TRIS PH 8.5, 30% POLYETHYLENE GLYCOL 4000, 200 MM SODIUM ACETATE TRIHYDRATE
Resolution 1.90 Å R-free 0.217
4E41 Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor G4 Deposited 2012-03-11 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain C 60–74(15 aa) Fragment:unp residues 60-74
Not recorded NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 8;298 K;20% (wt/vol) polyethylene glycol 1000, 0.2 M calcium acetate, 0.1 M imidazole, pH 8.0, VAPOR DIFFUSION, temperature 298K
Resolution 2.60 Å R-free 0.264
4E41 Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor G4 Deposited 2012-03-11 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain H 60–74(15 aa) Fragment:unp residues 60-74
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 8;298 K;20% (wt/vol) polyethylene glycol 1000, 0.2 M calcium acetate, 0.1 M imidazole, pH 8.0, VAPOR DIFFUSION, temperature 298K
Resolution 2.60 Å R-free 0.264
4POC Structure of Triosephosphate Isomerase Wild Type human enzyme. Deposited 2014-02-25 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 38–286(249 aa)
Chain B 38–286(249 aa)
Not recorded K POTASSIUM ION × 2 NA SODIUM ION × 1 BR BROMIDE ION × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;35% PEG 2000 MME, 0.05 KBr, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.60 Å R-free 0.187
4POD Structure of Triosephosphate Isomerase I170V mutant human enzyme. Deposited 2014-02-25 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 38–286(249 aa)
Chain B 38–286(249 aa)
Mutation:I170V Mutation:I170V K POTASSIUM ION × 2 NA SODIUM ION × 1 PO4 PHOSPHATE ION × 1 BR BROMIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;34% PEG 2000 MME, 0.05 KBr, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.99 Å R-free 0.213
4UNK Crystal structure of human triosephosphate isomerase (mutant N15D) Deposited 2014-05-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 39–286(248 aa) Fragment:RESIDUES 39-286
Chain B 39–286(248 aa) Fragment:RESIDUES 39-286
Mutation:YES Mutation:YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;200 MM AMMONIUM ACETATE, 100 MM TRIS PH 8.5, 25% V/VW/V POLYETHYLENE GLYCOL 3350
Resolution 2.00 Å R-free 0.224
4UNL Crystal structure of a single mutant (N71D) of triosephosphate isomerase from human Deposited 2014-05-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 39–286(248 aa) Fragment:RESIDUES 39-286
Chain B 39–286(248 aa) Fragment:RESIDUES 39-286
Mutation:YES Mutation:YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6;PROTEIN WAS CRYSTALLIZED FROM: 0.2 M AMMONIUM ACETATE, 0.1 M SODIUM CITRATE TRIBASIC DIHYDRATE PH 5.6, 30% W/V POLYETHYLENE GLYCOL 4,000
Resolution 1.50 Å R-free 0.226
4ZVJ Structure of human triose phosphate isomerase K13M Deposited 2015-05-18 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 38–286(249 aa)
Chain B 38–286(249 aa)
Mutation:K13M Mutation:K13M NA SODIUM ION × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;35% PEG 2000 MME, 50 mM KBr, Tris pH 7.5
Resolution 1.70 Å R-free 0.187
6C2G Human triosephosphate isomerase mutant V231M Deposited 2018-01-08 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 38–286(249 aa)
Chain C 38–286(249 aa)
Mutation:V231M Mutation:V231M No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.2 M Magnesium chloride hexahydrate, 0.1 M TRIS hydrochloride pH 8.5, 30% w/v Polyethylene glycol 4,000.
Resolution 2.30 Å R-free 0.226
6C2G Human triosephosphate isomerase mutant V231M Deposited 2018-01-08 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 38–286(249 aa)
Chain D 38–286(249 aa)
Mutation:V231M Mutation:V231M No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.2 M Magnesium chloride hexahydrate, 0.1 M TRIS hydrochloride pH 8.5, 30% w/v Polyethylene glycol 4,000.
Resolution 2.30 Å R-free 0.226
6D43 CHARACTERIZATION OF HUMAN TRIOSEPHOSPHATE ISOMERASE S-NITROSYLATION Deposited 2018-04-17 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 41–286(246 aa)
Chain B 41–286(246 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 2.04 Å R-free 0.256
6NLH Structure of human triose phosphate isomerase R189A Deposited 2019-01-08 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 42–286(245 aa)
Chain E 42–286(245 aa)
Mutation:R189A Mutation:R189A NA SODIUM ION × 4 BR BROMIDE ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;31% PEG 3350, 50 mM Potassium Bromide, Tris pH7.5
Resolution 2.20 Å R-free 0.216
6NLH Structure of human triose phosphate isomerase R189A Deposited 2019-01-08 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 42–286(245 aa)
Chain C 42–286(245 aa)
Mutation:R189A Mutation:R189A NA SODIUM ION × 7 BR BROMIDE ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;31% PEG 3350, 50 mM Potassium Bromide, Tris pH7.5
Resolution 2.20 Å R-free 0.216
6NLH Structure of human triose phosphate isomerase R189A Deposited 2019-01-08 Assembly 3 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 42–286(245 aa)
Chain F 42–286(245 aa)
Mutation:R189A Mutation:R189A NA SODIUM ION × 5 BR BROMIDE ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;31% PEG 3350, 50 mM Potassium Bromide, Tris pH7.5
Resolution 2.20 Å R-free 0.216
6NLH Structure of human triose phosphate isomerase R189A Deposited 2019-01-08 Assembly 4 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain G 42–286(245 aa)
Chain H 42–286(245 aa)
Mutation:R189A Mutation:R189A NA SODIUM ION × 4 BR BROMIDE ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;31% PEG 3350, 50 mM Potassium Bromide, Tris pH7.5
Resolution 2.20 Å R-free 0.216
6UP1 Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure Deposited 2019-10-16 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 39–286(248 aa)
Chain B 39–286(248 aa)
Not recorded IPA ISOPROPYL ALCOHOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283.15 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 1.83 Å R-free 0.261
6UP5 Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure Deposited 2019-10-16 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 39–286(248 aa)
Chain B 39–286(248 aa)
Not recorded GOL GLYCEROL × 3 IPA ISOPROPYL ALCOHOL × 3 PGA 2-PHOSPHOGLYCOLIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 1.92 Å R-free 0.232
6UP8 Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure Deposited 2019-10-16 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 39–286(248 aa)
Chain B 39–286(248 aa)
Mutation:F240L Mutation:F240L IPA ISOPROPYL ALCOHOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 2.00 Å R-free 0.253
6UPF Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure Deposited 2019-10-17 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 39–286(248 aa)
Chain B 39–286(248 aa)
Mutation:F240L Mutation:F240L PGA 2-PHOSPHOGLYCOLIC ACID × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.05 M Tris-HCl pH 7.5, 0.05 M NaCl, 1 mM EDTA, 15% PEG 4000 and 2 mM 2-PG
Resolution 1.65 Å R-free 0.197
7RDE Human Triose Phosphate Isomerase Q181P Deposited 2021-07-09 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–249(249 aa)
Chain B 1–249(249 aa)
Mutation:Q181P Mutation:Q181P BR BROMIDE ION × 2 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;30% PEG 3350, 50mM Potassium Bromide, Tris pH7.5
Resolution 1.31 Å R-free 0.162
7SX1 human triosephosphate isomerase mutant v154m Deposited 2021-11-22 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–249(249 aa)
Chain B 1–249(249 aa)
Mutation:V154M Mutation:V154M IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 2.23 Å R-free 0.225
7T0Q human triosephosphate isomerase mutant v154m Deposited 2021-11-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 2–249(248 aa)
Chain B 2–249(248 aa)
Mutation:V154M Mutation:V154M PGA 2-PHOSPHOGLYCOLIC ACID × 1 GOL GLYCEROL × 2 IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 2.00 Å R-free 0.206
7UXB Human triosephosphate isomerase mutant G122R Deposited 2022-05-05 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–249(249 aa)
Chain B 1–249(249 aa)
Mutation:G122R Mutation:G122R IPA ISOPROPYL ALCOHOL × 1 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol
Resolution 2.00 Å R-free 0.228
7UXV human triosephosphate isomerase mutant G122R Deposited 2022-05-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–249(249 aa)
Chain B 1–249(249 aa)
Mutation:G122R Mutation:G122R PGA 2-PHOSPHOGLYCOLIC ACID × 2 GOL GLYCEROL × 4 IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;283 K;0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-porpanol
Resolution 2.15 Å R-free 0.246
9F69 Crystal structure of human triose phosphate isomerase with methyl malonic acid ligand Deposited 2024-04-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 5–249(245 aa)
Not recorded DXX METHYLMALONIC ACID × 2 BR BROMIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;295 K;Protein buffer: 20 mM Tris pH 7.4, 30 mM NaCl. Reservoir: 0.14 M KBr, 24% PEG 2000 MME. Hanging drop: 1.5:1.5:1.0 ul - Reservoir-Protein (8 mg/ml)-Seed stock. Cryoprotectant = 20% glycerol; Ligand soaking performed for 5-6 min in a mixture containing 24 mM methylmalonate (pH adjusted to 7.4), mother liquor, and cryo-protectant Ligand soaking and cryoprotectant were performed simultaneously
Resolution 1.17 Å R-free 0.184
9FFC Crystal structure of human triose phosphate isomerase with glycerol-3-phosphate ligand Deposited 2024-05-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–249(249 aa)
Not recorded G3P SN-GLYCEROL-3-PHOSPHATE × 2 BR BROMIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.4;295 K;Protein buffer: 20 mM Tris pH 7.4, 30 mM NaCl. Reservoir: 0.14 M KBr, 24% PEG 2000 MME. Hanging drop: 1.5:1.5:1.0 ul - Reservoir-Protein (8 mg/ml)-Seed stock. Cryoprotectant = 20% glycerol; Ligand soaking performed for 5-6 min in a mixture containing 20 mM glycerol-3-phosphate (pH adjusted to 7.4), mother liquor, and cryo-protectant Ligand soaking and cryoprotectant were performed simultaneously
Resolution 1.25 Å R-free 0.180