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Yorodumi- PDB-3cd2: LIGAND INDUCED CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURES O... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3cd2 | ||||||
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Title | LIGAND INDUCED CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURES OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE COMPLEXES WITH FOLATE AND NADP+ | ||||||
Components | DIHYDROFOLATE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / OXIDO-REDUCTASE / METHOTREXATE / NADPH | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Cody, V. / Galitsky, N. / Rak, D. / Luft, J. / Pangborn, W. / Queener, S. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+. Authors: Cody, V. / Galitsky, N. / Rak, D. / Luft, J.R. / Pangborn, W. / Queener, S.F. #1: Journal: Structure (London) / Year: 1994 Title: THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION Authors: CHAMPNESS, J.N. / ACHARI, A. / BALLANTINE, S.P. / BRYANT, P.K. / DELVES, C.J. / 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 | 3cd2.cif.gz | 58.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3cd2.ent.gz | 42.2 KB | Display | PDB format |
PDBx/mmJSON format | 3cd2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cd/3cd2 ftp://data.pdbj.org/pub/pdb/validation_reports/cd/3cd2 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 23918.537 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH NADP+ AND FOLATE / Source: (gene. exp.) Pneumocystis carinii (fungus) / 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-NAP / |
#3: Chemical | ChemComp-MTX / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown / Details: temperature gradient | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Date: Jul 1, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→8 Å / Num. obs: 6691 / % possible obs: 96.3 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Rmerge(I) obs: 0.052 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 1.9→8 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 19.03 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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