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- PDB-4dfr: CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DI... -
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Basic information
Entry | Database: PDB / ID: 4dfr | |||||||||
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Title | CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE | |||||||||
![]() | DIHYDROFOLATE REDUCTASE | |||||||||
![]() | OXIDOREDUCTASE / OXIDO-REDUCTASE | |||||||||
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 | ![]() | |||||||||
![]() | Filman, D.J. / Matthews, D.A. / Bolin, J.T. / Kraut, J. | |||||||||
![]() | ![]() Title: Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. Authors: Bolin, J.T. / Filman, D.J. / Matthews, D.A. / Hamlin, R.C. / Kraut, J. #1: ![]() Title: Effect of Single Amino Acid Replacements on the Folding and Stability of Dihydrofolate Reductase from Escherichia Coli Authors: Perry, K.M. / Onuffer, J.J. / Touchette, N.A. / Herndon, C.S. / Gittelman, M.S. / Matthews, C.R. / Chen, J.-T. / Mayer, R.J. / Taira, K. / Benkovic, S.J. / Howell, E.E. / Kraut, J. #2: ![]() Title: Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase Refined 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. #3: ![]() Title: Crystal Structure of Avian Dihydrofolate Reductase Containing Phenyltriazine and Nadph Authors: Volz, K.W. / Matthews, D.A. / Alden, R.A. / Freer, S.T. / Hansch, C. / Kaufman, B.T. / Kraut, J. #4: ![]() Title: Interpretation of Nuclear Magnetic Resonance Spectra for Lactobacillus Casei Dihydrofolate Reductase Based on the X-Ray Structure of the Enzyme-Methotrexate-Nadph Complex Authors: Matthews, D.A. #5: ![]() Title: Dihydrofolate Reductase from Lactobacillus Casei. Stereochemistry of Nadph Binding Authors: Matthews, D.A. / Alden, R.A. / Freer, S.T. / Xuong, N.-H. / Kraut, J. #6: ![]() Title: Proton Magnetic Resonance Studies on Escherichia Coli Dihydrofolate Reductase. Assignment of Histidine C-2 Protons in Binary Complexes with Folates on the Basis of the Crystal Structure with ...Title: Proton Magnetic Resonance Studies on Escherichia Coli Dihydrofolate Reductase. Assignment of Histidine C-2 Protons in Binary Complexes with Folates on the Basis of the Crystal Structure with Methotrexate and on Chemical Modifications Authors: Poe, M. / Hoogsteen, K. / Matthews, D.A. #7: ![]() Title: Dihydrofolate Reductase from Lactobacillus Casei. X-Ray Structure of the Enzyme-Methotrexate-Nadph Complex Authors: Matthews, D.A. / Alden, R.A. / Bolin, J.T. / Filman, D.J. / Freer, S.T. / Hamlin, R. / Hol, W.G.J. / Kisliuk, R.L. / Pastore, E.J. / Plante, L.T. / Xuong, N.-H. / Kraut, J. #8: ![]() Title: Dihydrofolate Reductase. The Amino Acid Sequence of the Enzyme from a Methotrexate-Resistant Mutant of Escherichia Coli Authors: Bennett, C.D. / Rodkey, J.A. / Sondey, J.M. / Hirschmann, R. #9: ![]() Title: Dihydrofolate Reductase. X-Ray Structure of the Binary Complex with Methotrexate Authors: Matthews, D.A. / Alden, R.A. / Bolin, J.T. / Freer, S.T. / Hamlin, R. / Xuong, N. / Kraut, J. / Poe, M. / Williams, M. / Hoogsteen, K. #10: ![]() Title: Dihydrofolate Reductase. Purification and Characterization of the Enzyme from an Amethopterin-Resistant Mutant of Escherichia Coli Authors: Poe, M. / Greenfield, N.J. / Hirshfield, J.M. / Williams, M.N. / Hoogsteen, K. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.3 KB | Display | ![]() |
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PDB format | ![]() | 67.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 510.4 KB | Display | ![]() |
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Full document | ![]() | 627.7 KB | Display | |
Data in XML | ![]() | 23.4 KB | Display | |
Data in CIF | ![]() | 32.2 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: SEE REMARK 8. / 2: SEE REMARK 9. / 3: SEE REMARK 10. / 4: SEE REMARK 11. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.92116, -0.37966, 0.636818), Vector: Details | THE MTRIX TRANSFORMATION PRESENTED BELOW WILL SUPERIMPOSE MOLECULE B ON MOLECULE A. | |
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Components
#1: Protein | Mass: 18020.393 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 | RESIDUE 142 IS LISTED AS ASN IN THE SEQUENCE PAPER (SEE REFERENCE 9 ABOVE). THE X-RAY STRUCTURE ...RESIDUE 142 IS LISTED AS ASN IN THE SEQUENCE PAPER (SEE REFERENCE 9 ABOVE). THE X-RAY STRUCTURE SUGGESTS IT IS ASP (EVIDENCE IS INTERMOLEC | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 51.93 % | ||||||||||||||||||||
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Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||
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: 1.7 Å / Num. obs: 32554 / % possible obs: 88 % |
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Processing
Refinement | Rfactor Rwork: 0.155 / Highest resolution: 1.7 Å Details: MOLECULE DESIGNATED AS CHAIN B BELOW IS PREFERRED FOR STRUCTURAL COMPARISONS BECAUSE IT IS MORE COMPLETE AND LESS PERTURBED BY INTERMOLECULAR CONTACTS. ALTERNATE LOCATIONS *A* AND *B* ARE ...Details: MOLECULE DESIGNATED AS CHAIN B BELOW IS PREFERRED FOR STRUCTURAL COMPARISONS BECAUSE IT IS MORE COMPLETE AND LESS PERTURBED BY INTERMOLECULAR CONTACTS. ALTERNATE LOCATIONS *A* AND *B* ARE PARTIALLY OCCUPIED CONFORMATIONS FOR RESIDUES SER A 64, SER A 150, HIS B 45, SER B 64 AND ASP B 122. IN ALL CASES, *A* IS BELIEVED TO BE THE MAJOR CONFORMER. NEITHER THE OCCUPANCIES NOR THE THERMAL PARAMETERS SHOULD BE CONSIDERED AS RELIABLE. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 1.7 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.7 Å / Num. reflection all: 32554 / Rfactor obs: 0.155 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |