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Yorodumi- PDB-1m7a: CANDIDA ALBICANS DIHYDROFOLATE REDUCTASE COMPLEXED WITH DIHYDRO-N... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1m7a | ||||||
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Title | CANDIDA ALBICANS DIHYDROFOLATE REDUCTASE COMPLEXED WITH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (NADPH) AND 7-[2-methoxy-1-(methoxymethyl)ethyl]-7H-pyrrolo[3,2-f] quinazoline-1,3-diamine (GW557) | ||||||
Components | DIHYDROFOLATE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / ANTIFUNGAL TARGET / REDUCTASE | ||||||
Function / homology | Function and homology information 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 | Candida albicans (yeast) | ||||||
Method | X-RAY DIFFRACTION / DIRECT REPLACEMENT / Resolution: 1.76 Å | ||||||
Authors | Whitlow, M. / Howard, A.J. / Kuyper, L.F. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1997 Title: X-Ray Crystallographic Studies of Candida Albicans Dihydrofolate Reductase. High Resolution Structures of the Holoenzyme and an Inhibited Ternary Complex. Authors: Whitlow, M. / Howard, A.J. / Stewart, D. / Hardman, K.D. / Kuyper, L.F. / Baccanari, D.P. / Fling, M.E. / Tansik, R.L. #1: Journal: J.Med.Chem. / Year: 2001 Title: X-Ray Crystal Structures of Candida Albicans Dihydrofolate Reductase: High Resolution Ternary Complexes in which the Dihydronicotinamide Moiety of Nadph is Displaced by an Inhibitor Authors: Whitlow, M. / Howard, A.J. / Stewart, D. / Hardman, K.D. / Chan, J.H. / Baccanari, D.P. / Tansik, R.L. / Hong, J.S. / Kuyper, L.F. #2: Journal: J.Med.Chem. / Year: 1995 Title: Selective Inhibitors of Candida Albicans Dihydrofolate Reductase: Activity and Selectivity of 5-(Arylthio)-2,4-Diaminoquinazolines Authors: Chan, J.H. / Hong, J.S. / Kuyper, L.F. / Baccanari, D.P. / Joyner, S.S. / Tansik, R.L. / Boytos, C.M. / Rudolph, S.K. #3: Journal: J.Biol.Chem. / Year: 1989 Title: Characterization of Candida Albicans Dihydrofolate Reductase Authors: Baccanari, D.P. / Tansik, R.L. / Joyner, S.S. / Fling, M.E. / Smith, P.L. / Freisheim, J.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1m7a.cif.gz | 105 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1m7a.ent.gz | 80.5 KB | Display | PDB format |
PDBx/mmJSON format | 1m7a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1m7a_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 1m7a_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 1m7a_validation.xml.gz | 24.2 KB | Display | |
Data in CIF | 1m7a_validation.cif.gz | 33.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m7/1m7a ftp://data.pdbj.org/pub/pdb/validation_reports/m7/1m7a | HTTPS FTP |
-Related structure data
Related structure data | 1ai9SC 1aoeC 1m78C 1m79C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | Dihydrofolate reductase is active as a monomer. |
-Components
#1: Protein | Mass: 22194.527 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida albicans (yeast) / Gene: DFR1 / Plasmid: P1869 / Species (production host): Escherichia coli / Cellular location (production host): cytoplasm / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P22906, dihydrofolate reductase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 43 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: dihydro-nicotinamide-adenine-dinucleotide phosphate (NADPH), 7-[2-METHOXY-1-(METHOXYMETHYL)ETHYL]-7H-PYRROLO[3,2-F] QUINAZOLINE-1,3-DIAMINE (GW557), PEG-3350, Potassium 4- ...Details: dihydro-nicotinamide-adenine-dinucleotide phosphate (NADPH), 7-[2-METHOXY-1-(METHOXYMETHYL)ETHYL]-7H-PYRROLO[3,2-F] QUINAZOLINE-1,3-DIAMINE (GW557), PEG-3350, Potassium 4-morphilineethanesulfonic acid (MES), dithiothreitol (DTT), pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 / Wavelength: 1.5418 Å |
Detector | Type: XENTRONICS / Detector: AREA DETECTOR / Date: May 6, 1989 / Details: Huber Graphite MONOCHROMATOR |
Radiation | Monochromator: HUBER GRAPHITE MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.76→50 Å / Num. obs: 36247 / % possible obs: 94.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.18 % / Biso Wilson estimate: 31.86 Å2 / Rmerge(I) obs: 0.0552 / Rsym value: 0.0552 / Net I/σ(I): 18.55 |
Reflection shell | Resolution: 1.76→1.83 Å / Redundancy: 1.693 % / Rmerge(I) obs: 0.193 / Mean I/σ(I) obs: 2.77 / Num. unique all: 4590 / Rsym value: 0.193 / % possible all: 72.76 |
-Processing
Software |
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Refinement | Method to determine structure: DIRECT REPLACEMENT Starting model: CANDIDA ALBICANS DHFR (PDB ENTRY 1AI9) Resolution: 1.76→10 Å Isotropic thermal model: Konnert, J.H. & Hendrickson, W.A. (1980) Acta Crystallogr. A A36, 344. Cross valid method: NONE / σ(F): 2 / σ(I): -3 Stereochemistry target values: Hendrickson, W.A. (1985) Methods Enzymol. 115 252-270. Details: RESTRAIN LEAST-SQUARES PROCEDURE.
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Refinement step | Cycle: LAST / Resolution: 1.76→10 Å
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Refine LS restraints |
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LS refinement shell |
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