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Open data
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Basic information
Entry | Database: PDB / ID: 8tim | ||||||
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Title | TRIOSE PHOSPHATE ISOMERASE | ||||||
![]() | TRIOSE PHOSPHATE ISOMERASE | ||||||
![]() | ISOMERASE / GLYCOLYSIS / GLUCONEOGENESIS / FATTY ACID BIOSYNTHESIS | ||||||
Function / homology | ![]() Glycolysis / Glycolysis / Gluconeogenesis / Gluconeogenesis / methylglyoxal biosynthetic process / methylglyoxal synthase / methylglyoxal synthase activity / triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process ...Glycolysis / Glycolysis / Gluconeogenesis / Gluconeogenesis / methylglyoxal biosynthetic process / methylglyoxal synthase / methylglyoxal synthase activity / triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / canonical glycolysis / glycerol catabolic process / gluconeogenesis / glycolytic process / ubiquitin protein ligase binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Artymiuk, P.J. / Taylor, W.R. / Phillips, D.C. | ||||||
![]() | ![]() Title: Triose Phosphate Isomerase Authors: Artymiuk, P.J. / Taylor, W.R. / Phillips, D.C. #1: ![]() Title: Human Triosephosphate Isomerase Deficiency Resulting from Mutation of Phe-240 Authors: Chang, M.L. / Artymiuk, P.J. / Wu, X. / Hollan, S. / Lammi, A. / Maquat, L.E. #2: ![]() Title: Human Triose-Phosphate Isomerase Deficiency: A Single Amino Acid Substitution Results in a Thermolabile Enzyme Authors: Daar, I.O. / Artymiuk, P.J. / Phillips, D.C. / Maquat, L.E. #3: ![]() Title: On the Three-Dimensional Structure and Catalytic Mechanism of Triose Phosphate Isomerase Authors: Alber, T. / Banner, D.W. / Bloomer, A.C. / Petsko, G.A. / Phillips, D. / Rivers, P.S. / Wilson, I.A. #4: ![]() Title: Atomic Coordinates for Triose Phosphate Isomerase from Chicken Muscle Authors: Banner, D.W. / Bloomer, A.C. / Petsko, G.A. / Phillips, D.C. / Wilson, I.A. #5: ![]() Title: Studies of the Histidine Residues of Triose Phosphate Isomerase by Proton Magnetic Resonance and X-Ray Crystallography Authors: Browne, C.A. / Campbell, I.D. / Kiener, P.A. / Phillips, D.C. / Waley, S.G. / Wilson, I.A. #8: ![]() Title: Structure of Chicken Muscle Triose Phosphate Isomerase Determined Crystallographically at 2.5 Angstrom Resolution Using Amino Acid Sequence Data Authors: Banner, D.W. / Bloomer, A.C. / Petsko, G.A. / Phillips, D.C. / Pogson, C.I. / Wilson, I.A. / Corran, P.H. / Furth, A.J. / Milman, J.D. / Offord, R.E. / Priddle, J.D. / Waley, S.G. #9: ![]() Title: Crystallographic Studies of Chicken Triose Phosphate Isomerase Authors: Banner, D.W. / Bloomer, A.C. / Petsko, G.A. / Phillips, D.C. / Pogson, C.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.3 KB | Display | ![]() |
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PDB format | ![]() | 80.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 395 KB | Display | ![]() |
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Full document | ![]() | 458.5 KB | Display | |
Data in XML | ![]() | 19.2 KB | Display | |
Data in CIF | ![]() | 27 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.72691, 0.09842, -0.67964), Vector: |
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Components
#1: Protein | Mass: 26540.289 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | CHICKEN TRIOSE PHOSPHATE ISOMERASE HAS 247 AMINO ACID RESIDUES. THEY ARE NUMBERED 2-248 FOR EASE OF ...CHICKEN TRIOSE PHOSPHATE ISOMERASE HAS 247 AMINO ACID RESIDUES. THEY ARE NUMBERED 2-248 FOR EASE OF COMPARISON | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.61 % |
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Crystal grow | pH: 7 / Details: pH 7 |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Type: OTHER / Wavelength: 1.5418 |
Detector | Type: HILGER-WATTS / Detector: DIFFRACTOMETER / Date: Apr 1, 1975 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→10 Å / Num. obs: 17023 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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