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Open data
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Basic information
Entry | Database: PDB / ID: 1vie | ||||||
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Title | STRUCTURE OF DIHYDROFOLATE REDUCTASE | ||||||
![]() | DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / NADP / TRIMETHOPRIM RESISTANCE / METHOTREXATE RESISTANCE / ONE-CARBON METABOLISM / PLASMID | ||||||
Function / homology | ![]() response to methotrexate / dihydrofolate reductase / dihydrofolate reductase activity / tetrahydrofolate biosynthetic process / one-carbon metabolic process / response to xenobiotic stimulus / response to antibiotic Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Narayana, N. / Matthews, D.A. / Howell, E.E. / Xuong, N.-H. | ||||||
![]() | ![]() Title: A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site. Authors: Narayana, N. / Matthews, D.A. / Howell, E.E. / Nguyen-huu, X. #1: ![]() Title: Does R67 Dihydrofolate Reductase Possess a Proton Donor? Authors: Holland, J.C. / Linn, C.E. / Digiammarino, E. / Nichols, R. / Howell, E.E. #2: ![]() Title: Construction of a Synthetic Gene for an R-Plasmid-Encoded Dihydrofolate Reductase and Studies on the Role of the N-Terminus in the Protein Authors: Reece, L.J. / Nichols, R. / Ogden, R.C. / Howell, E.E. #3: ![]() Title: Crystal Structure of a Novel Trimethoprim-Resistant Dihydrofolate Reductase Specified in Escherichia Coli by R-Plasmid R67 Authors: Matthews, D.A. / Smith, S.L. / Baccanari, D.P. / Burchall, J.J. / Oatley, S.J. / Kraut, J. #4: ![]() Title: The Amino Acid Sequence of the Trimethoprim-Resistant Dihydrofolate Reductase Specified in Escherichia Coli by R-Plasmid R67 Authors: Stone, D. / Smith, S.L. #5: ![]() Title: Trimethoprim Resistance Determined by R Factors Authors: Fleming, M.P. / Datta, N. / Gruneberg, R.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 25.2 KB | Display | ![]() |
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PDB format | ![]() | 15.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 360.2 KB | Display | ![]() |
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Full document | ![]() | 361.2 KB | Display | |
Data in XML | ![]() | 2.9 KB | Display | |
Data in CIF | ![]() | 4.1 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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Components
#1: Protein | Mass: 6732.528 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: TMP-RESISTANT, CONTAINING R67 DHFR OVERPRODUCING PLASMID PLZ1 Gene: SYNTHETIC GENE / Plasmid details: PLZ1 / Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Compound details | R67 PLASMID-ENCODED DHFR HAS 78 AMINO ACID RESIDUES. THE PRESENT STUDY DESCRIBES THE TRUNCATED FORM ...R67 PLASMID-ENCODED DHFR HAS 78 AMINO ACID RESIDUES. THE PRESENT STUDY DESCRIBES THE TRUNCATED FORM OF R67 DHFR (62 RESIDUES) OBTAINED BY CLEAVING THE FULL-LENGTH PROTEIN AT PHE 16 USING CHYMOTRYPS |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: CRYSTALS WERE GROWN FROM HANGING- DROPS CONTAINING PROTEIN AT A FINAL CONCENTRATION OF ABOUT 15 MG/ML IN 100 MM TRIS-HCL BUFFER AT PH 7.5 AND 25% 2-METHYL-2,4-PENTANEDIOL (MPD). DROPS WERE ...Details: CRYSTALS WERE GROWN FROM HANGING- DROPS CONTAINING PROTEIN AT A FINAL CONCENTRATION OF ABOUT 15 MG/ML IN 100 MM TRIS-HCL BUFFER AT PH 7.5 AND 25% 2-METHYL-2,4-PENTANEDIOL (MPD). DROPS WERE EQUILIBRATED AGAINST A RESERVOIR CONTAINING 100 MM KH2PO4 BUFFER AT PH 6.8 AND 50% MPD., vapor diffusion - hanging drop PH range: 6.8-7.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Oct 15, 1991 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→10 Å / Num. obs: 7060 / % possible obs: 98 % / Observed criterion σ(I): 4 / Redundancy: 4 % / Biso Wilson estimate: 10.4 Å2 / Rsym value: 0.036 / Net I/σ(I): 13 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 3 % / Mean I/σ(I) obs: 3 / Rsym value: 0.1095 / % possible all: 97 |
Reflection | *PLUS Rmerge(I) obs: 0.036 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 18.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å / Luzzati d res low obs: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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