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- PDB-1ag1: MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE IS... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ag1 | ||||||
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Title | MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE | ||||||
![]() | TRIOSEPHOSPHATE ISOMERASE | ||||||
![]() | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) / ISOMERASE (INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | ![]() glycosome / triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / gluconeogenesis / glycolytic process / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Verlinde, C.L.M.J. / Hol, W.G.J. | ||||||
![]() | ![]() Title: Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate. Authors: Verlinde, C.L. / Noble, M.E. / Kalk, K.H. / Groendijk, H. / Wierenga, R.K. / Hol, W.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.2 KB | Display | ![]() |
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PDB format | ![]() | 82.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 392.4 KB | Display | ![]() |
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Full document | ![]() | 412.1 KB | Display | |
Data in XML | ![]() | 13.4 KB | Display | |
Data in CIF | ![]() | 20.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6timS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 26865.832 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | ChemComp-PO4 / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.59 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 2.4 M AMMONIUM SULFATE IN 0.2 MOPS BUFFER, PH 7.0 FOLLOWED BY TRANSFER TO 44% PEG-6000 CONTAINING 15 MM PHOSPHATE | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop / Details: Wierenga, R.K., (1984) J. Mol. Biol., 178, 487. | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Mar 1, 1990 / Details: STANDARD |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.36 Å / Num. obs: 17592 / % possible obs: 87.5 % / Observed criterion σ(I): 2 / Redundancy: 1.7 % / Rmerge(I) obs: 0.063 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 6TIM Resolution: 2.36→6 Å / Isotropic thermal model: TNT BCORREL V1.0 / Cross valid method: A POSTERIORI / σ(F): 3 / Stereochemistry target values: TNT PROTGEO /
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Refinement step | Cycle: LAST / Resolution: 2.36→6 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5C / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.15 / Rfactor Rwork: 0.15 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |