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- PDB-1dhi: LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dhi | ||||||
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Title | LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT DIHYDROFOLATE REDUCTASE | ||||||
![]() | 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 | ![]() | ||||||
![]() | Oatley, S.J. / Villafranca, J.E. / Brown, K.A. / Kraut, J. | ||||||
![]() | ![]() Title: Long-range structural effects in a second-site revertant of a mutant dihydrofolate reductase. Authors: Brown, K.A. / Howell, E.E. / Kraut, J. #1: ![]() Title: How Do Mutation at Phenylalanine-153 and Isoleucine-155 Partially Suppress the Effects of the Aspartate-27-> Serine Mutation in Escherichia Coli Dihydrofolate Reductase Authors: Dion, A. / Linn, C.E. / Bradrick, T.D. / Georghiou, S. / Howell, E.E. #2: ![]() Title: Role of Aspartate 27 of Dihydrofolate Reductase from Escherichia Coli in Interconversion of Active and Inactive Enzyme Conformers and the Binding of Nadph Authors: Appleman, J.R. / Howell, E.E. / Kraut, J. / Blakely, R.L. #3: ![]() Title: A Second-Site Mutation at Phenylalanine-137 that Increases Catalytic Efficiency in the Mutant Aspartate-27-> Serine Escherichia Coli Dihydrofolate Reductase Authors: Howell, E.E. / Booth, C. / Farnum, M. / Kraut, J. / Warren, M.S. #4: ![]() Title: Dihydrofolate Reductase from Escherichia Coli: Probing the Role of Aspartate-27 and Phenylalanine-137 in Enzyme Conformation and the Binding of Nadph Authors: Dunn, S.M. / Lanigan, T.M. / Howell, E.E. #5: ![]() Title: Functional Role of Aspartic Acid-27 in Dihydrofolate Reductase Revealed by Mutagenesis Authors: Howell, E.E. / Villafranca, J.E. / Waren, M.S. / Oatley, S.J. / Kraut, J. #6: ![]() Title: Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase at 1.7 Angstroms Resolution. I. General Features and Binding of Methotrexate Authors: Bolin, J.T. / Filman, D.J. / Matthews, D.A. / Hamlin, R.C. / Kraut, J. #7: ![]() Title: Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase at 1.7 Angstroms Resolution. II. Environment of Bound Nadph and Implications for Catalysis Authors: Filman, D.J. / Bolin, J.T. / Matthews, D.A. / Kraut, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 87.8 KB | Display | ![]() |
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PDB format | ![]() | 66.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 497.9 KB | Display | ![]() |
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Full document | ![]() | 514.6 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Data in CIF | ![]() | 17.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Atom site foot note | 1: GLY A 95 - GLY A 96 OMEGA = 2.83 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: GLY B 95 - GLY B 96 OMEGA = 2.85 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.9245, -0.37489, 0.06906), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO CHAIN *B*. | |
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Components
#1: Protein | Mass: 17992.316 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-CA / | #5: Water | ChemComp-HOH / | Sequence details | SEQUENCE ADVISORY NOTICE: DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: ...SEQUENCE ADVISORY NOTICE: DIFFERENCE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.2 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.8 / Method: unknown / Details: referred to J.Biol.Chem. 257.13650-13662 1982 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 26345 / % possible obs: 91 % / Rmerge(I) obs: 0.06 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.155 / Highest resolution: 1.9 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.9 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Num. reflection obs: 26345 / Rfactor obs: 0.155 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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