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Yorodumi- PDB-1dyr: THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dyr | ||||||
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Title | THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION | ||||||
Components | DIHYDROFOLATE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / OXIDO-REDUCTASE | ||||||
Function / homology | Function and homology information glycine biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding Similarity search - Function | ||||||
Biological species | Pneumocystis carinii (fungus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.86 Å | ||||||
Authors | Champness, J.N. / Achari, A. / Ballantine, S.P. / Bryant, P.K. / Delves, C.J. / Stammers, D.K. | ||||||
Citation | Journal: Structure / Year: 1994 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: Journal: J.Mol.Biol. / Year: 1993 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: Journal: Protein Expr.Purif. / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dyr.cif.gz | 61 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dyr.ent.gz | 43.6 KB | Display | PDB format |
PDBx/mmJSON format | 1dyr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dy/1dyr ftp://data.pdbj.org/pub/pdb/validation_reports/dy/1dyr | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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 |
-Components
#1: Protein | Mass: 23918.537 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pneumocystis carinii (fungus) / Description: RAT-DERIVED / Gene: C-DNA P.CARINII DHFR / Plasmid: PT7-7 / Gene (production host): C-DNA P.CARINII DHFR / Production host: Escherichia coli (E. coli) / References: UniProt: P16184, dihydrofolate reductase |
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#2: Chemical | ChemComp-NDP / |
#3: Chemical | ChemComp-TOP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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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 |
-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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