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- PDB-1dyr: THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dyr | ||||||
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Title | THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION | ||||||
![]() | DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / OXIDO-REDUCTASE | ||||||
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 | ![]() | ||||||
![]() | Champness, J.N. / Achari, A. / Ballantine, S.P. / Bryant, P.K. / Delves, C.J. / Stammers, D.K. | ||||||
![]() | ![]() Title: The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution. Authors: Champness, J.N. / Achari, A. / Ballantine, S.P. / Bryant, P.K. / Delves, C.J. / Stammers, D.K. #1: ![]() Title: Preliminary Crystallographic Data for Pneumocystis Carinii Dihydrofolate Reductase Authors: Stammers, D.K. / Delves, C. / Ballantine, S. / Jones, E.Y. / Stuart, D.I. / Achari, A. / Bryant, P.K. / Champness, J.N. #2: ![]() Title: Refolding of Recombinant Pneumocystis Carinii Dihydrofolate Reductase and Characterization of the Enzyme Authors: Delves, C.J. / Ballantine, S.P. / Tansik, R.L. / Baccanari, D.P. / Stammers, D.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 | ![]() | 61 KB | Display | ![]() |
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PDB format | ![]() | 43.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 518.6 KB | Display | ![]() |
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Full document | ![]() | 528.2 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 11.1 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: CIS PROLINE - PRO 71 2: GLY 124 - GLY 125 OMEGA = 1.21 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 23918.537 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NDP / |
#3: Chemical | ChemComp-TOP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.99 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: vapor diffusion, sitting drop / Details: Stammers, D.K., (1993) J.Mol.Biol., 230, 679. | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: SIEMENS / Date: Jun 24, 1992 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 15602 / % possible obs: 83 % / Observed criterion σ(I): 2 / Redundancy: 2.7 % / Rmerge(I) obs: 0.05 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. measured all: 41714 / Rmerge(I) obs: 0.05 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.91 Å / % possible obs: 39 % / Num. unique obs: 1193 / Mean I/σ(I) obs: 2.61 |
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Processing
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Refinement | Resolution: 1.86→10 Å /
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Displacement parameters | Biso mean: 23.08 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.86→10 Å
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Refine LS restraints |
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