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- PDB-1e26: Design, Synthesis and X-ray Crystal Structure of a Potent Dual In... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1.0E+26 | ||||||
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Title | Design, Synthesis and X-ray Crystal Structure of a Potent Dual Inhibitor of Thymidylate Synthase and Dihydrofolate Reductase as an Antitumor Agent. | ||||||
![]() | DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / DIHYDROFOLATE REDUCTASE / THYMIDYLATE SYNTHASE | ||||||
Function / homology | ![]() dihydrofolate metabolic process / glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gangjee, A. / Yu, J. / McGuire, J.J. / Cody, V. / Galitsky, N. / Kisliuk, R.L. / Queener, S.F. | ||||||
![]() | ![]() Title: Ligand-Induced Conformational Changes in the Crystal Structures of Pneumocystis Carinii Dihydrofolate Reductase Complexes with Folate and Nadp+ Authors: Cody, V. / Galitsky, N. / Rak, D. / Luft, J.R. / Pangborn, W. / Queener, S.F. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. STRANDS 1 TO 7 SHEETS A AND A1 ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.3 KB | Display | ![]() |
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PDB format | ![]() | 43.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 524.5 KB | Display | ![]() |
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Full document | ![]() | 536.4 KB | Display | |
Data in XML | ![]() | 8.5 KB | Display | |
Data in CIF | ![]() | 11.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cd2C ![]() 2cd2SC ![]() 3cd2C ![]() 4cd2C S: Starting model for refinement C: citing same article ( |
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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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Components
#1: Protein | Mass: 23918.537 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH NADPH AND INHIBITOR / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-GPB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||
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Crystal grow | Method: microbatch / pH: 6 Details: PROTEIN SOLUTION: WASHED AND CONCENTRATED 4 TUBES PCDHFR USING A CENTRICON 10 50 MM MES, 100MM KCL, B-NADPH, PH 6.0, A280/340 RATIO OF 24. WASHED WITH 50MM MES, 100MM KCL, PH 6.0, WASHED ...Details: PROTEIN SOLUTION: WASHED AND CONCENTRATED 4 TUBES PCDHFR USING A CENTRICON 10 50 MM MES, 100MM KCL, B-NADPH, PH 6.0, A280/340 RATIO OF 24. WASHED WITH 50MM MES, 100MM KCL, PH 6.0, WASHED WITH 50MM MES, 100MM KCL, PH 6.0 TO A CONCENTRATION OF 6.5 MG/ML. RESERVOIR SOLUTION: 50% PEG2000MME, 50MM MES, 100MM, PH 6.0 SET UP MICROBATCH POLYTHERMAL GRADIENT EXPERIMENTS IN MICROPETS. DROPS WERE COMPOSED OF: 2.5 MICROLITERS PROTEIN SOLUTION 2.0 MICROLITERS PROTEIN SOLUTION 0.5 MICROLITERS 50MM MES, 100MM KCL, PH 6.0. MICROPETS WERE LEFT TO EQUILIBRATE ON THE POLYTHERMAL GRADIENT. | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→100 Å / Num. obs: 11919 / % possible obs: 99.4 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Rmerge(I) obs: 0.054 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 50 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.049 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.1 Å / % possible obs: 99.4 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2CD2 Resolution: 2→100 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: THE C-TERMINAL MET RESIDUE WAS NOT SEEN IN THE DENSITY MAPS
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Refinement step | Cycle: LAST / Resolution: 2→100 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS_SOLVE / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 50 Å / Num. reflection obs: 11919 / Rfactor obs: 0.223 / Rfactor Rfree: 0.297 / Rfactor Rwork: 0.223 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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