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- PDB-1tdr: EXPRESSION, CHARACTERIZATION, AND CRYSTALLOGRAPHIC ANALYSIS OF TE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tdr | ||||||
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Title | EXPRESSION, CHARACTERIZATION, AND CRYSTALLOGRAPHIC ANALYSIS OF TELLUROMETHIONYL DIHYDROFOLATE REDUCTASE | ||||||
![]() | TELLUROMETHIONYL DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
Function / homology | ![]() methotrexate binding / dihydrofolic acid binding / response to methotrexate / NADP+ binding / folic acid binding / dihydrofolate metabolic process / glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process ...methotrexate binding / dihydrofolic acid binding / response to methotrexate / NADP+ binding / folic acid binding / dihydrofolate metabolic process / glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / NADPH binding / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding / response to xenobiotic stimulus / response to antibiotic / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lewinski, K. / Lebioda, L. | ||||||
![]() | ![]() Title: Expression, characterization and crystallographic analysis of telluromethionyl dihydrofolate reductase. Authors: Boles, J.O. / Lewinski, K. / Kunckle, M.G. / Hatada, M. / Lebioda, L. / Dunlap, R.B. / Odom, J.D. #1: ![]() Title: Bio-Incorporation of Telluromethionine Into Buried Residues of Dihydrofolate Reductase Authors: Boles, J.O. / Lewinski, K. / Kunkle, M. / Odom, J.D. / Dunlap, R.B. / Lebioda, L. / Hatada, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 88 KB | Display | ![]() |
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PDB format | ![]() | 65.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 505.1 KB | Display | ![]() |
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Full document | ![]() | 552.8 KB | Display | |
Data in XML | ![]() | 16.4 KB | Display | |
Data in CIF | ![]() | 22.6 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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Unit cell |
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Atom site foot note | 1: GLY A 95 - GLY A 96 OMEGA = 359.20 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: GLY B 95 - GLY B 96 OMEGA = 359.75 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 18020.393 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P00379, UniProt: P0ABQ4*PLUS, dihydrofolate reductase |
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-Non-polymers , 5 types, 349 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/MTX.gif)
![](data/chem/img/TE.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MTX.gif)
![](data/chem/img/TE.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-TE / #5: Chemical | ChemComp-CA / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.27 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Detector: CCD / Date: Oct 24, 1992 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Num. obs: 11234 / % possible obs: 88 % / Redundancy: 4.35 % / Rmerge(I) obs: 0.068 |
Reflection | *PLUS Highest resolution: 2.5 Å / Num. measured all: 48880 / Rmerge(I) obs: 0.065 |
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Processing
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Refinement | Resolution: 2.5→16 Å / σ(F): 0 Details: ATOM SD OF MET 42 AND ATOM SD OF MET 92 HAVE BEEN PARTIALLY CHEMICALLY SUBSTITUTED BY TELLURIUM. COORDINATES ARE GIVEN FOR BOTH SD AND TE IN THIS ENTRY, WITH PARTIAL OCCUPANCIES. NOTE THAT ...Details: ATOM SD OF MET 42 AND ATOM SD OF MET 92 HAVE BEEN PARTIALLY CHEMICALLY SUBSTITUTED BY TELLURIUM. COORDINATES ARE GIVEN FOR BOTH SD AND TE IN THIS ENTRY, WITH PARTIAL OCCUPANCIES. NOTE THAT IT IS NOT POSSIBLE FOR BOTH SD AND TE TO BE PRESENT SIMULTANEOUSLY IN ONE RESIDUE. ATOMS SD MET 42 AND SD MET 92 ARE PRESENTED AS PART OF RESIDUES 42 AND 92, RESPECTIVELY. THE TELLURIUM ATOMS ARE PRESENTED AS HET GROUPS AT THE END OF THE CHAIN.
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Refinement step | Cycle: LAST / Resolution: 2.5→16 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.124 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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